Academic literature on the topic 'Polypeptides'

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Journal articles on the topic "Polypeptides":

1

Darr, S. C., S. C. Somerville, and C. J. Arntzen. "Monoclonal antibodies to the light-harvesting chlorophyll a/b protein complex of photosystem II." Journal of Cell Biology 103, no. 3 (September 1, 1986): 733–40. http://dx.doi.org/10.1083/jcb.103.3.733.

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A collection of 17 monoclonal antibodies elicited against the light-harvesting chlorophyll a/b protein complex which serves photosystem II (LHC-II) of Pisum sativum shows six classes of binding specificity. Antibodies of two of the classes recognize a single polypeptide (the 28- or the 26- kD polypeptides), thereby suggesting that the two proteins are not derived from a common precursor. Other classes of antibodies cross-react with several polypeptides of LHC-II or with polypeptides of both LHC-II and the light-harvesting chlorophyll a/b polypeptides of photosystem I (LHC-I), indicating that there are structural similarities among the polypeptides of LHC-II and LHC-I. The evidence for protein processing by which the 26-, 25.5-, and 24.5-kD polypeptides are derived from a common precursor polypeptide is discussed. Binding studies using antibodies specific for individual LHC-II polypeptides were used to quantify the number of antigenic polypeptides in the thylakoid membrane. 27 copies of the 26-kD polypeptide and two copies of the 28-kD polypeptide were found per 400 chlorophylls. In the chlorina f2 mutant of barley, and in intermittent light-treated barley seedlings, the amount of the 26-kD polypeptide in the thylakoid membranes was greatly reduced, while the amount of 28-kD polypeptide was apparently not affected. We propose that stable insertion and assembly of the 28-kD polypeptide, unlike the 26-kD polypeptide, is not regulated by the presence of chlorophyll b.
2

Machesky, L. M., S. J. Atkinson, C. Ampe, J. Vandekerckhove, and T. D. Pollard. "Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin-agarose." Journal of Cell Biology 127, no. 1 (October 1, 1994): 107–15. http://dx.doi.org/10.1083/jcb.127.1.107.

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We identified four polypeptides of 47, 44, 40, and 35 kD that bind to profilin-Sepharose and elute with high salt. When purified by conventional chromatography using an antibody to the 47-kD polypeptide, these four polypeptides copurified as a stoichiometric complex together with three additional polypeptides of 19, 18, and 13 kD that varied in their proportions to the other polypeptides. Partial protein sequences showed that the 47-kD polypeptide is a homologue of S. pombe act2 and the 44-kD polypeptide is a homologue of S. cerevisiae ACT2, both unconventional actins. The 40-kD polypeptide contains a sequence similar to the WD40 motif of the G beta subunit of a trimeric G-protein from Dictyostelium discoideum. From partial sequences, the 35-, 19-, and 18-kD polypeptides appear to be novel proteins. On gel filtration the complex of purified polypeptides cochromatograph with a Stokes' radius of 4.8 nm, a value consistent with a globular particle of 220 kD containing one copy of each polypeptide. Cell extracts also contain components of the complex that do not bind the profilin column. Affinity purified antibodies localize 47- and 18/19-kD polypeptides in the cortex and filopodia of Acanthamoeba. Antibodies to the 47-kD unconventional actin cross-react on immunoblots with polypeptides of similar size in Dictyostelium, rabbit muscle, and conventional preparations of rabbit muscle actin but do not react with actin.
3

Geysen, J., J. Cardoen, and A. De Loof. "Distribution of yolk polypeptides in the follicle cells during the differentiation of the follicular epithelium in Sarcophaga bullata egg follicles." Development 101, no. 1 (September 1, 1987): 33–43. http://dx.doi.org/10.1242/dev.101.1.33.

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In S. bullata, the ovaries contribute to the synthesis of yolk polypeptides. A specific antiserum for yolk polypeptides was used to visualize the presence of yolk polypeptides in the follicle cells during their differentiation. After vitellogenesis has started, all follicle cells contain yolk polypeptides. The squamous follicle cells covering the nurse cells and the border cells lose yolk polypeptides before mid-vitellogenesis, whereas the follicle cells over the oocyte contain yolk polypeptides until after late vitellogenesis. All follicle cells are immunonegative afterwards. In vitro translation of poly(A)+ RNA demonstrated that the presence of yolk polypeptide mRNA correlates well with follicle cell immunopositivity for yolk polypeptides. This suggests that the follicle cells synthesize the ovarian yolk polypeptides. Differences in cellular and nuclear morphology, total and poly(A)+ RNA synthesis and the rate of yolk polypeptide synthesis were shown to be correlated with the presence or absence of yolk polypeptides in the differentiating follicular epithelium. The possible relationship between these different aspects of follicle cell differentiation, follicle cell polyploidy and the extracellular current pattern around follicles are discussed.
4

Bodnar, Andrea G., and Richard A. Rachubinski. "Characterization of the integral membrane polypeptides of rat liver peroxisomes isolated from untreated and clofibrate-treated rats." Biochemistry and Cell Biology 69, no. 8 (August 1, 1991): 499–508. http://dx.doi.org/10.1139/o91-074.

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We have characterized the integral membrane polypeptides of liver peroxisomes from untreated rats and rats treated with clofibrate, a peroxisome proliferator. Membranes, prepared by treatment of purified peroxisomes with sodium carbonate, were used to raise an antiserum in rabbits. Immunoblot analysis demonstrated the reaction of this antiserum with six peroxisomal integral membrane polypeptides (molecular masses, 140, 69, 50, 36, 22, and 15 kDa). Treatment of rats with the hypolipidemic drug clofibrate caused a 4- to 10-fold induction in the 69-kDa integral membrane polypeptide, while the other integral membrane polypeptides remained unchanged or varied to a lesser extent. The anti-peroxisomal membrane serum reacted with two integral membrane polypeptides of the endoplasmic reticulum which co-migrated with the 50- and 36-kDa integral membrane polypeptides of the peroxisome. Biochemical and immunoblot analyses indicated that these integral membrane polypeptides were co-localized to peroxisomes and endoplasmic reticulum. Immunoprecipitation of in vitro translation products of RNA isolated from free and membrane-bound polysomes indicated that the 22-, 36-, and 69-kDa integral membrane polypeptides were synthesized on free polysomes, while the 50-kDa integral membrane polypeptide was predominantly synthesized on membrane-bound polysomes. The predominant synthesis of the 50-kDa integral membrane polypeptide on membrane-bound polysomes raises interesting possibilities concerning its biosynthesis.Key words: peroxisomes, integral membrane polypeptides, clofibrate, free polysomes, membrane-bound polysomes.
5

Newsted, W. J., and N. P. A. Huner. "Major polypeptides associated with differentiation in psychrophilic fungi." Canadian Journal of Botany 65, no. 2 (February 1, 1987): 233–41. http://dx.doi.org/10.1139/b87-033.

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Major polypeptides were observed upon one-dimensional sodium dodecyl sulfate gel electrophoresis of sclerotial extracts of the following psychrophiles: Myriosclerotinia borealis, Coprinus psychromorbidus, Typhula idahoensis, and Typhula incarnata. In general, the number, molecular mass, and relative proportion of these major sclerotial polypeptides varied considerably from species to species. Furthermore, in the case of M. borealis, the major sclerotial polypeptide did not appear to be an artifact of culturing conditions since a major polypeptide of similar molecular mass was also present in sclerotia of M. borealis collected from the field. Generally, the major sclerotial polypeptides were visible in the sclerotial initials but were not apparent in the vegetative hyphae. Thus, these major sclerotial polypeptides appear to be expressed as a function of sclerotial development. Electrophoresis of protein extracts of T. idahoensis and T. incarnata initially solubilized either in sodium dodecyl sulfate or urea sample buffer indicated that the type of denaturant initially used had a profound influence on the relative proportions of the major polypeptides and the overall polypeptide profile. Isoelectric focusing of sclerotial extracts indicated that the isoelectric points of the major sclerotial polypeptides of M. borealis ranged from 6.2 to 6.7, whereas the values of the major sclerotial polypeptides of the other three species were basic and ranged from 7.0 to 7.7.
6

Wheeler, R. A., Rex L. Smith, and D. A. Knauft. "Microsomal Polypeptide Comparisons Between High and Normal Oleic Acid Isogenic Peanut Lines Using Two-Dimensional Gel Electrophoresis1." Peanut Science 21, no. 1 (January 1, 1994): 75–78. http://dx.doi.org/10.3146/i0095-3679-21-1-17.

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Abstract Peanut (Arachis hypogaea L. subsp. fastigiata var. vulgaris) developing seed microsomal polypeptides of the high oleic acid variant (F435) and its presumed isogenic, normal line (78-1339) were compared using two-dimensional gel electrophoresis. A pair of 20 kDa polypeptides focusing at pH 6.8 and 7.3 was present in all of the polypeptide profiles from both isolines regardless of maturity or genotype except for (F435) at stage 1 maturity. The stage 1 (F435) profile contained, instead, an 18 kDa polypeptide pair focusing at about pH 9.3. Based on correlation evidence, we postulate that the 20 kDa polypeptides could be components of the $DT12-desaturase complex. The 18 kDa polypeptides appeared to be associated with lower desaturase activity, reduced linoleic acid and increased oleic acid seed content. Since the 18 kDa polypeptides focusing at pH 9.3 are not found at later stages, they are probably under developmental control. Changes in the developing seed polypeptides of the microsomal fraction over the four maturities are also reported.
7

Kim, W. K., N. K. Howes, and J. W. Martens. "Evidence for relatedness between Puccinia graminis f.sp. secalis and P. graminis f.sp. tritici from two-dimensional polypeptide mapping." Canadian Journal of Botany 65, no. 6 (June 1, 1987): 1078–82. http://dx.doi.org/10.1139/b87-149.

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Two-dimensional electrophoretograms of detergent-soluble polypeptides extracted from dormant urediospores were used to compare interspecific and intraspecific relationships among nine races of rye stem rust (Puccinia graminis f.sp. secalis) and a hybrid between rye stem rust and wheat stem rust (P. graminis f.sp. tritici) and its parents. More than 280 polypeptides were detected in each race of rye stem rust. The nine races differed by one to five genes for virulence and by five to seven polypeptides, but these differences were not correlated. The rye–wheat stem rust hybrid, rye stem rust parent, and wheat stem rust parent differed by 12 polypeptides. The polypeptide patterns of the rye stem rust races were similar to those previously found for wheat and oat stem rusts. Rye stem rust and wheat stem rust had 270 polypeptides in common and differed by 17 polypeptides. In contrast, 92 polypeptides separated rye and oat stem rusts. The considerable homology in polypeptide patterns is consistent with the view that these three cereal stem rusts are related and that rye stem rust and wheat stem rust have the closest genetic relationship.
8

Kawchuk, L. M., W. K. Kim, and J. Nielsen. "A comparison of polypeptides from the wheat bunt fungi Tilletia laevis, T. tritici, and T. controversa." Canadian Journal of Botany 66, no. 12 (December 1, 1988): 2367–76. http://dx.doi.org/10.1139/b88-321.

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Phenol-soluble polypeptides were extracted from teliospores of six races of each of Tilletia laevis and T. tritici, and eight collections of T. controversa. The polypeptides were separated by two-dimensional isoelectric focusing – polyacrylamide gel electrophoresis and the resulting patterns compared. Although the races and collections had the morphological and physiological features of their respective species and possessed different combinations of virulence genes, they all gave similar polypeptide patterns. There were 359 polypeptides common to all 20 races and collections. Another 56 polypeptides were found in only some races and collections, but none of these variable polypeptides were species specific, i.e., found in every race or collection of one species but absent from every race or collection of one or both of the other species. Therefore, no polypeptide could be correlated to a morphological or physiological feature typical of any one species. Furthermore, no correlation was found between the polypeptides and virulence. However, previous studies on interspecific hybridization, the overlap in spore morphology and germination requirements, and the high number of common polypeptides and absence of species-specific polypeptides demonstrated here prove a closer genetic relationship among the three fungi than is indicated by their current taxonomic designation. It is, therefore, proposed to treat them as varieties of one species: T. tritici var. laevis, T. tritici var. tritici, and T. tritici var. controversa.
9

Dentler, W. L. "Fractionation of Tetrahymena ciliary membranes with triton X-114 and the identification of a ciliary membrane ATPase." Journal of Cell Biology 107, no. 6 (December 1, 1988): 2679–88. http://dx.doi.org/10.1083/jcb.107.6.2679.

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Cilia were isolated from Tetrahymena thermophila, extracted with Triton X-114, and the detergent-soluble membrane + matrix proteins separated into Triton X-114 aqueous and detergent phases. The aqueous phase polypeptides include a high molecular mass polypeptide previously identified as a membrane dynein, detergent-soluble alpha and beta tubulins, and numerous polypeptides distinct from those found in axonemes. Integral membrane proteins partition into the detergent phase and include two major polypeptides of 58 and 50 kD, a 49-kD polypeptide, and 5 polypeptides in relatively minor amounts. The major detergent phase polypeptides are PAS-positive and are phosphorylated in vivo. A membrane-associated ATPase, distinct from the dynein-like protein, partitions into the Triton X-114 detergent phase and contains nearly 20% of the total ciliary ATPase activity. The ATPase requires Mg++ or Ca++ and is not inhibited by ouabain or vanadate. This procedure provides a gentle and rapid technique to separate integral membrane proteins from those that may be peripherally associated with the matrix or membrane.
10

Enrich, C., O. Bachs, and W. H. Evans. "A 115 kDa calmodulin-binding protein is located in rat liver endosome fractions." Biochemical Journal 255, no. 3 (November 1, 1988): 999–1005. http://dx.doi.org/10.1042/bj2550999.

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The distribution of calmodulin-binding polypeptides in various rat liver subcellular fractions was investigated. Plasma-membrane, endosome, Golgi and lysosome fractions were prepared by established procedures. The calmodulin-binding polypeptides present in the subcellular fractions were identified by using an overlay technique after transfer from gels to nitrocellulose sheets. Distinctive populations of calmodulin-binding polypeptides were present in all the fractions examined except lysosomes. A major 115 kDa calmodulin-binding polypeptide of pI 4.3 was located to the endosome subfractions, and it emerges as a candidate endosome-specific protein. Partitioning of endosome fractions between aqueous and Triton X-114 phases indicated that the calmodulin-binding polypeptide was hydrophobic. Major calmodulin-binding polypeptides of 140 and 240 kDa and minor polypeptides of 40-60 kDa were present in plasma membranes. The distribution of calmodulin in the various endosome and plasma-membrane fractions was also analysed, and the results indicated that the amounts were high compared with those in the cytosol.

Dissertations / Theses on the topic "Polypeptides":

1

Aronsson, Christopher. "Tunable and modular assembly of polypeptides and polypeptide-hybrid biomaterials." Doctoral thesis, Linköpings universitet, Molekylär fysik, 2016. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-132949.

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Biomaterials are materials that are specifically designed to be in contact with biological systems and have for a long time been used in medicine. Examples of biomaterials range from sophisticated prostheses used for replacing outworn body parts to ordinary contact lenses. Currently it is possible to create biomaterials that can e.g. specifically interact with cells or respond to certain stimuli. Peptides, the shorter version of proteins, are excellent molecules for fabrication of such biomaterials. By following and developing design rules it is possible to obtain peptides that can self-assemble into well-defined nanostructures and biomaterials. The aim of this thesis is to create ”smart” and tunable biomaterials by molecular self-assembly using dimerizing –helical polypeptides. Two different, but structurally related, polypeptide-systems have been used in this thesis. The EKIV-polypeptide system was developed in this thesis and consists of four 28-residue polypeptides that can be mixed-and-matched to self-assemble into four different coiled coil heterodimers. The dissociation constant of the different heterodimers range from μM to < nM. Due to the large difference in affinities, the polypeptides are prone to thermodynamic social self-sorting. The JR-polypeptide system, on the other hand, consists of several 42-residue de novo designed helix-loop-helix polypeptides that can dimerize into four-helix bundles. In this work, primarily the glutamic acid-rich polypeptide JR2E has been explored as a component in supramolecular materials. Dimerization was induced by exposing the polypeptide to either Zn2+, acidic conditions or the complementary polypeptide JR2K. By conjugating JR2E to hyaluronic acid and the EKIV-polypeptides to star-shaped poly(ethylene glycol), respectively, highly tunable hydrogels that can be self-assembled in a modular fashion have been created. In addition, self-assembly of spherical superstructures has been investigated and were obtained by linking two thiol-modified JR2E polypeptides via a disulfide bridge in the loop region. ŒThe thesis also demonstrates that the polypeptides and the polypeptide-hybrids can be used for encapsulation and release of molecules and nanoparticles. In addition, some of the hydrogels have been explored for 3D cell culture. By using supramolecular interactions combined with bio-orthogonal covalent crosslinking reactions, hydrogels were obtained that enabled facile encapsulation of cells that retained high viability. The results of the work presented in this thesis show that dimerizing α–helical polypeptides can be used to create modular biomaterials with properties that can be tuned by specific molecular interactions. The modularity and the tunable properties of these smart biomaterials are conceptually very interesting andmake them useful in many emerging biomedical applications, such as 3D cell culture, cell therapy, and drug delivery .
2

Göransson, Ulf. "Macrocyclic polypeptides from plants." Doctoral thesis, Uppsala University, Department of Medicinal Chemistry, 2002. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-1956.

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The aim of this work was to explore the structural and functional diversity of polypeptides that are found in plants. Expanding knowledge of simililarities between plant use of these compound and animal use promises exceptional opportunities for finding, from plant research, new structures with biomedical and biotechnological potential.

A fractionation protocol was developed and applied to many plant species, providing fractions enriched in polypeptides, amenable to chemical and biological evaluation. From one species, the common field pansy (Viola arvensis), a 29-amino-acid residue polypeptide was isolated, named varv A, which revealed a remarkable macrocyclic structure (i.e., N- and C-termini are joined) stabilised by three knotted disulfides.

Varv A, together with an increasing number of homologous peptides, form the currently known peptide family of cyclotides. Their stable structure makes them an attractive scaffold for protein engineering. In addition, they display a wide range of biological activities (e.g., antimicrobial, cytotoxic, and insecticidal). As a part of this work, the cytotoxic effects of varv A and two other isolated cyclotides were evaluated in a human cell-line panel: all were active in the low µM range. Most likely, these effects involve pore formation through cell membranes.

Cyclotides were found to be common in the plant family Violaceae; with eleven cyclotides isolated and sequenced from V. arvensis, V. cotyledon, and Hybanthus parviflorus. For six members of the genus Viola, cyclotide expression profiles were examined by liquid chromatography-mass spectrometry (LC-MS): all expressed notably complex mixtures, with single species containing more than 50 cyclotides. These profiles reflect the evolution of the genus.

To assess these mixtures, a rational strategy for MS based amino acid sequencing of cyclotides was developed, circumventing inherent structural problems, such as low content of positively charged amino acids and the macrocyclic structure. This was achieved by aminoethylation of cysteines, which, following tryptic digestion, produced fragments of size and charge amenable to MS analysis. This method was also modified and used for mapping of disulfide bonds.

Methods for isolation and characterisation developed in this work may prove useful not only for further studies on macrocyclic polypeptides from plants, but also for other plant peptides and disulfide-rich peptides from animals.

3

Ng, Yuen-lam Stephanie, and 吳宛霖. "Identification of VIP, PACAP and their receptors in agnathans: insights into the ancestral origin of theligands and receptors." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2010. http://hub.hku.hk/bib/B45704879.

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Mortenson, Paul Neil. "Energy landscapes of model polypeptides." Thesis, University of Cambridge, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.621232.

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Monreal, Jorge. "Polymer Characteristics of Polyelectrolyte Polypeptides." Scholar Commons, 2016. http://scholarcommons.usf.edu/etd/6326.

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Polypeptides are polymerized chains of amino acids linked covalently through peptide bonds. Polyelectrolyte polypeptides are polypeptides with electrolyte repeating groups. Several amino acids contain ionizable side chains which result in charge distributions when dissolved in aqueous solutions. This dissertation is motivated by a desire to gain knowledge of polyelectrolyte polypeptides as recent advances in chemical synthesis of polypeptides have made possible the fabrication of designed polypeptides that do not naturally occur in nature. Potential applications of newly designed polypeptides span the range from medical to clothing and energy even to robotics. In this dissertation we compare the characteristic behavior of two polypeptide polyanions: Poly-(L-Glutamic Acid) [PLE] and Poly-(L-Glutamic Acid4, Tyrosine1) [PLEY(4:1)]. Comparative characteristic behaviors of each is conducted through relaxation phenomena in the context of mechanical elasticity measurements of hydrogels and dielectric relaxation of aqueous solutions in a radio frequency range of 1 MHz to 1000 MHz. Hydrogels are fabricated by crosslinking each polyanion with Poly-(L-Lysine) [PLK], a polycation, via the crosslinker 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride (EDC). Elasticity and viscoelasticity measurements are conducted in a fixture designed by our lab. Dielectric relaxation behavior is studied on aqueous solution of both PLEY and PLE using a capacitive fixture, also designed in our lab. RF signals provided by an impedance analyzer are converted to permittivity and dielectric loss measurements. Peaks in dielectric loss provide evidence of relaxation mechanisms. A comparison of experimental results to theoretical expectations reveal both expected and some surprising behavior. Relaxation times for crosslinked hydro-gels scale according to theoretical expectations according to so-called reptation dynamics. However, relaxation times of aqueous solutions did not scale as entangled polyelectrolytes. First, both PLEY and PLE scaled as neutral polymers rather than polyelectrolytes. This was expected because of the high concentrations studied. However, due to the high concentrations, it was expected that polypeptides were entangled in solutions. Data compared to theory did not support this expectation. We, additionally, conducted a self-crosslinking experiment of a polyampholyte: RADA16. RADA16 is known to self-assemble into nano-fibers formed by -sheet stacking. The self-crosslinking was also mediated by EDC. Results of crosslinking showed formation of polypeptide spherules as well as nano-crystals nominally orthorhombic in shape. It was not possible to ascertain composition of the nano-crystals due to both the limited amount of raw material available and the capabilities of measurement equipment as of this writing. It is hypothesized that nano-crystals are composed of some type of urea by-product from the crosslinking reaction. The spherules, on the other hand, seem to be described by the theory of hydrophobic polyelectrolytes. Additional research conducted with regards to electromagnetic hydrodynamic flows during the time frame of this dissertation is also included. The research uses hydrodynamic conservation equations as a starting point to derive one electromagnetic flow momentum equation analogous to the Cauchy momentum equation of hydrodynamics. It also introduces a mass- energy conservation equation for electromagnetic flow that has no hydrodynamic analogue. We begin this dissertation by introducing in Chapter 1 some of the theoretical background necessary to understand results from experiments. Chapter 2 introduces experimental results from elasticity and viscoelasticity measurements and Chapter 3 explains the dielectric relaxation experiment. We then follow with Chapter 4 which presents conclusions from mechanical and dielectric relaxation experiments in a concise format. Results from the self- crosslinking of RADA16 are presented in Chapter 5. Finally, the additional research on electromagnetic flow is presented in Chapter 6.
6

Crick, F. "Polypeptides and proteins : X-ray studies." Thesis, University of Cambridge, 2013. https://www.repository.cam.ac.uk/handle/1810/250994.

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Oomen, Ray. "Interaction of polypeptides with lipid bilayers." Thesis, University of Ottawa (Canada), 1988. http://hdl.handle.net/10393/5253.

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Ling, Roger. "Polypeptides of murine and avian pneumoviruses." Thesis, University of Warwick, 1988. http://wrap.warwick.ac.uk/55532/.

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The work described in this thesis identifies some properties of the major polypeptides of pneumonia virus of mice (PVM) and of turkey rhinotracheitis (TRT) virus. The PVM glycoproteins have been studied in particular detail while the results obtained with TRT virus provide a preliminary description of the polypeptides of this virus. Twelve major PVM specific polypeptides designated L, G1, G2, F1, N, 39K, 35K, M, 20K, 19K, 16K and 12K were identified. In addition PVM specific polypeptides designated 25K, 24K, 23K, 18K and 17K were sometimes detected. Monoclonal antibodies directed against the G1/G2, 39K and M polypeptides were produced. The a~ility of a monoclonal antibody to precipitate G1 and G2 suggested that these two glycosylated proteins were related and this was confirmed by tryptic peptide mapping. G2 was shown to be derived from G1 in pulse chase experiments and a similar relationship between two higher mobility polypeptides synthesized in the presence of tunicamycin was observed. The G protein may have a precursor since G1 did not appear immediately following a pulse labelling. The precursor could not however be identified. An additional minor glycosylated polypeptide of 42K was found to be related to the G protein. The F1 protein appeared to be poorly glycosylated and a difference in mobility of the polypeptide synthesized in the presence of tunicamycin did not appear to be directly due to a lack of N-linked oligosaccharides. The polypeptide migrated more slowly under non-reducing conditions but no evidence of a small disulphide bonded polypeptide was found in contrast to the situation with other paramyxoviruses. This polypeptide appeared to be the major PVM protein expressed on the cell surface and was associated with G1 and G2 as the major protein in a particulate fraction of the infected cell supernatant. Tentative relationships were suggested between the 39K, 35K and 25K polypeptides, the M and 24K polypeptides and the 20K and 19K polypeptides. This together with the observation that the 12K polypeptide was not a primary gene product suggested that there may be about 11 PVM polypeptides. The N or 39K and the 20K or 19K polypeptides were observed to be phosphorylated. Twelve possible TRT virus specific polypeptides of 150K, 129K, 95K, 83K, 57K, 45K, 38K, 35K, 3DK, 23K, 19K and 15K were identified. The 150K, 95K, 83K, 57K, 45K and 15K polypeptides were glycosylated with the latter three polypeptides showing a similar relationship to the F1,2, F1 and F2 polypeptides of paramyxoviruses. A broad glycosylated band designated the 31K polypeptide was identified that was similar to a smeared band observed on prolonged exposure of immunoprecipitates of PVM polypeptides labelled with [3H]-glucosamine. The 35K and 19K polypeptides were observed to be phosphorylated. PVM may be more closely related to RS virus than TRT virus since anti-PVM serum irnmunoprecipitated the RS virus N polypeptide but not any TRT virus polypeptides. The PVM 39K polypeptide and the RS virus P protein were recognised by a monoclonal antibody providing further evidence of a relationship between PVM and RS virus.
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Galbraith, Toby Patrick. "Biophysical studies of membrane channel polypeptides." Thesis, Birkbeck (University of London), 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.249171.

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Mullin, M. J. "Combinatorial studies on the B-loop residues of human epidermal growth factor." Thesis, Queen's University Belfast, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.273233.

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Books on the topic "Polypeptides":

1

Ito, Koreaki, ed. Regulatory Nascent Polypeptides. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-55052-5.

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Van Regenmortel, M. H. V., ed. Synthetic polypeptides as antigens. Amsterdam: Elsevier, 1988.

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Ling, Roger. Polypeptides of murine and avian pneumoviruses. [s.l.]: typescript, 1988.

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Yakubovich, Alexander V. Theory of Phase Transitions in Polypeptides and Proteins. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-22592-5.

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Yakubovich, Alexander V. Theory of Phase Transitions in Polypeptides and Proteins. Berlin, Heidelberg: Springer-Verlag Berlin Heidelberg, 2011.

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Wallis, M. The biochemistry of the polypeptide hormones. Chichester: Wiley, 1985.

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1943-, Hider R. C., and Barlow D. 1954-, eds. Polypeptide and protein drugs: Production, charactrerization, and formulation. New York: Horwood, 1991.

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1943-, Hider R. C., and Barlow D. 1954-, eds. Polypeptide and protein drugs: Production, characterization and formulation. New York: Ellis Horwood, 1991.

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Galoyan, Armen. Brain immune system signal molecules in protection from aerobic and anaerobic infections. New York: Springer, 2012.

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Wood, Katherine Anne. A preproabrin: Genomic cloning and expression of the constituent polypeptides in heterologous systems. [s.l.]: typescript, 1991.

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Book chapters on the topic "Polypeptides":

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Ciardelli, Francesco, Simona Bronco, Osvaldo Pieroni, and Andrea Pucci. "Photoswitchable Polypeptides." In Molecular Switches, 321–60. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2011. http://dx.doi.org/10.1002/9783527634408.ch10.

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van Eldijk, Mark B., Christopher L. McGann, Kristi L. Kiick, and Jan C. M. van Hest. "Elastomeric Polypeptides." In Topics in Current Chemistry, 71–116. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/128_2011_205.

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Sisido, Masahiko. "Chromophoric Polypeptides." In ACS Symposium Series, 343–57. Washington, DC: American Chemical Society, 1987. http://dx.doi.org/10.1021/bk-1987-0358.ch026.

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Bährle-Rapp, Marina. "Saccharomyces Polypeptides." In Springer Lexikon Kosmetik und Körperpflege, 485. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-71095-0_9042.

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Ito, Koreaki, and Shinobu Chiba. "Biological Significance of Nascent Polypeptides That Stall the Ribosome." In Regulatory Nascent Polypeptides, 3–20. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-55052-5_1.

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Vázquez-Laslop, Nora, and Alexander S. Mankin. "Triggering Peptide-Dependent Translation Arrest by Small Molecules: Ribosome Stalling Modulated by Antibiotics." In Regulatory Nascent Polypeptides, 165–86. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-55052-5_10.

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Yamashita, Yui, Noriyuki Onoue, Katsunori Murota, Hitoshi Onouchi, and Satoshi Naito. "Translation Elongation Arrest Induced by S-Adenosyl-l-Methionine-Sensing Nascent Peptide in Plants." In Regulatory Nascent Polypeptides, 187–201. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-55052-5_11.

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Palanimurugan, R., Leo Kurian, Vishal Hegde, Kay Hofmann, and R. Jürgen Dohmen. "Co-translational Polyamine Sensing Co-translational polyamine sensing by Nascent ODC Antizyme ODC antizyme." In Regulatory Nascent Polypeptides, 203–22. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-55052-5_12.

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Woolstenhulme, Christopher J., and Allen R. Buskirk. "Isolation of Ribosome Stalling Motifs from Random Libraries." In Regulatory Nascent Polypeptides, 225–40. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-55052-5_13.

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Bernstein, Harris D. "The Coupling of SecA Expression to Secretion Efficiency by SecM-Mediated Translation Arrest." In Regulatory Nascent Polypeptides, 241–56. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-55052-5_14.

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Conference papers on the topic "Polypeptides":

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Bloom, J. W., J. A. Berkner, and G. Mitra. "FACTOR VIII:C, 80 KD AND 90-210 KD POLYPEPTIDE QUANTITATION BY SLISA." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644042.

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Abstract:
Purified Factor VIII:c is generally found proteolyzed into nultiple polypeptides. An 80 kD polypeptide appears to form a metal-linked complex with each of a series of 90-210 kD polypeptides and separation of these complexes results in loss af Factor VIII:c activity. To quantitate total Factor VIII:c content - active and inactive - three sandwich ELISA's were developed using an immunopurified polyclonal antibody as the capture antibody. This antibody was shown by a Western blot of Factor VIII:c to interact with all the 80-210 kD polypeptides. Utilizing biotinylated polyclonal antibody, an ELISA was developed that detected both the purified carboxy terminal (80 kD) and amino terminal (90-210 kD) polypeptides. Thrombin treated 80 kD polypeptide and Factor VIII:c were also detected by this ELISA. A second ELISA was developed with a biotinylated monoclonal, designated C8, that detected purified 90-210 kD polypeptides, but not the 80 kD polypeptide. A third ELISA was developed with a biotinylated monoclonal, designated C7F7, that detected only the purified 80 kD functional subunit of Factor VIII:c. Thrombin treated 80 kD polypeptide and Factor VIII:c were not detected by this ELISA. These three ELISA methods combined allow estimates of amounts of denatured or thrombin degraded Factor VIII:c to be determined, information not obtainable by the coagulation activity assays.
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Fay, P. J. "THROMBIN-ACTIVATED FACTOR VIIIa IS COMPOSED OF A NONCOVALENT 73/51 kD DIMER." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644040.

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Abstract:
Human factor VIII purified from plasma concentrates consists of a series of heterodimers composed of a light chain of 83 kD noncovalently bound to a heavy chain which varies in size from 93 to 170 kD. Previously, we showed that each of the purified heterodimers wasactivated by thrombin to a similar extent. Activation to factor VIIIa was correlated with proteolysis of the light chain generating a73 kD polypeptide and cleavage of the heavy chain(s) generating polypeptides of 51 and 43 kD, whereas subsequent inactivation of factor VIIIa occurred in the absence of further proteolysis (Biochim Biophys Acta 871:268-278, 1986). SDS-polyacrylamide gel electrophoresis (SDS-PAGE) of reduced or nonreduced samples showed similar polypeptide patterns indicating that there were no covalent linkages between the 51 and 43 kD chains. However, prior data does not distinguish between a factor VIIIa complex of the 73, 51 and 43 kD polypeptides and a subset of these chains. To identify factor VIIIa, thrombin- treated factor VIII at peak activity was subjected to rapid gel filtration on Superose 12. Factor VIII activity eluted as a single peak representing about 30% of the applied activity after correction for spontaneous inactivation. SDS-PAGE followedby silver staining showed that activity was correlated to fractionscontaining the 73 and 51 kD polypeptides, which co-eluted and which were separated from both the 43 kD fragment and thrombin. Densitometric scans of the stained gel indicated the stoichiometry of the 73:51 kD polypeptides in eachactive fraction to be 1:1. Addition of EDTA(50 mM) to a similar thrombin-factor VIII mixture resulted in rapid inactivation of factor VIIIa. Gel filtration followed by SDS-PAGE analysis of this sample showed that the 73 and 51 kD polypeptides eluted separately and were more included, while the elution position of the 43 kD polypeptide was unchanged. These results suggest that factor VIIIa is represented by a noncovalent dimer consisting of a 73 kD polypeptide derivedfrom the light chain plus a 51 kD polypeptide derived from the heavy chain.
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Williams, Lance R. "Programs as Polypeptides." In European Conference on Artificial Life 2015. The MIT Press, 2015. http://dx.doi.org/10.7551/978-0-262-33027-5-ch033.

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Lee, Benjamin W., Rajib Schubert, Yuk Kee Cheung, Federico Zannier, Qian Wei, Daniele Sacchi, and Samuel K. Sia. "Multivalent polypeptides for tunable cell adhesion." In 2010 36th Annual Northeast Bioengineering Conference. IEEE, 2010. http://dx.doi.org/10.1109/nebc.2010.5458113.

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Valiaev, Alexei, Robert L. Clark, Ashutosh Chilkoti, and Stefan Zauscher. "Conformational mechanics of stimulus-responsive polypeptides." In Smart Structures and Materials, edited by Dimitris C. Lagoudas. SPIE, 2003. http://dx.doi.org/10.1117/12.484700.

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Parameswaran, GI, S. Sethi, and TF Murphy. "Antimicrobial Polypeptides and Moraxella Catarrhalis in COPD." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a3225.

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Reynaud, J. A., A. Brack, J. P. Grivet, and Y. Trudelle. "Interaction of phospholipids with basic amphiphilic polypeptides." In The living cell in four dimensions. AIP, 1991. http://dx.doi.org/10.1063/1.40574.

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Rousslang, Kenneth W., Steve K. Buratto, D. Haynes, P. Heath, D. Holloway, John C. Hulteen, Lisa Dick, K. Stevenson, C. O. Harding, and J. B. Alexander Ross. "Time-resolved phosphorescence of proteins and polypeptides." In OE/LASE '90, 14-19 Jan., Los Angeles, CA, edited by Joseph R. Lakowicz. SPIE, 1990. http://dx.doi.org/10.1117/12.17735.

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Cooper, Thomas M., Morley O. Stone, Keith A. Obermeier, Robert L. Crane, Bob L. Epling, Zbigniew Tokarski, and Lalgudi V. Natarajan. "Second-harmonic generation in corona-poled polypeptides." In OE/LASE'93: Optics, Electro-Optics, & Laser Applications in Science& Engineering, edited by Peter M. Rentzepis. SPIE, 1993. http://dx.doi.org/10.1117/12.144059.

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KANG, HYE-JIN, JIN-HEE KIM, EUNG-SOO KIM, and YOON-MO KOO. "RECOVERY OF LEVANSUCRASE USING ELASTIN-LIKE POLYPEPTIDES." In Proceedings of the 4th International Conference. WORLD SCIENTIFIC, 2004. http://dx.doi.org/10.1142/9789812702623_0147.

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Reports on the topic "Polypeptides":

1

Lamb, C. J. Biosynthesis of plant plasmamembrane polypeptides. Office of Scientific and Technical Information (OSTI), January 1992. http://dx.doi.org/10.2172/5688524.

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2

Urry, Dan W. Production of Elastomeric Polypeptides for Materials Characterizations. Fort Belvoir, VA: Defense Technical Information Center, February 2004. http://dx.doi.org/10.21236/ada420503.

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Lamb, C. J. Biosynthesis of plant plasmamembrane polypeptides. [Final technical report]. Office of Scientific and Technical Information (OSTI), April 1992. http://dx.doi.org/10.2172/10134950.

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Garrison, W. M. Reaction mechanisms in the radiolysis of peptides, polypeptides and proteins. Office of Scientific and Technical Information (OSTI), January 1985. http://dx.doi.org/10.2172/5415209.

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Mevarech, Moshe, Jeremy Bruenn, and Yigal Koltin. Virus Encoded Toxin of the Corn Smut Ustilago Maydis - Isolation of Receptors and Mapping Functional Domains. United States Department of Agriculture, September 1995. http://dx.doi.org/10.32747/1995.7613022.bard.

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Abstract:
Ustilago maydis is a fungal pathogen of maize. Some strains of U. maydis encode secreted polypeptide toxins capable of killing other susceptible strains of U. maydis. Resistance to the toxins is conferred by recessive nuclear genes. The toxins are encoded by genomic segments of resident double-strande RNA viruses. The best characterized toxin, KP6, is composed of two polypeptides, a and b, which are not covalently linked. It is encoded by P6M2 dsRNA, which has been cloned, sequenced and expressed in a variety of systems. In this study we have shown that the toxin acts on the membranes of sensitive cells and that both polypeptides are required for toxin activity. The toxin has been shown to function by creating new pores in the cell membrane and disrupting ion fluxes. The experiments performed on artificial phospholipid bilayers indicated that KP6 forms large voltage-independent, cation-selective channels. Experiments leading to the resolution of structure-function relationship of the toxin by in vitro analysis have been initiated. During the course of this research the collaboration also yielded X-ray diffracion data of the crystallized a polypeptide. The effect of the toxin on the pathogen has been shown to be receptor-mediated. A potential receptor protein, identified in membrane fractions of sensitive cells, was subjected to tryptic hydrolysis followed by amino-acid analysis. The peptides obtained were used to isolate a cDNA fragment by reverse PCR, which showed 30% sequence homology to the human HLA protein. Analysis of other toxins secreted by U. maydis, KP1 and KP4, have demonstrated that, unlike KP6, they are composed of a single polypeptide. Finally, KP6 has been expressed in transgenic tobacco plants, indicating that accurate processing by Kex2p-like activity occurs in plants as well. Using tobacco as a model system, we determined that active antifungal toxins can be synthesized and targeted to the outside of transgenic plant cells. If this methodology can be applied to other agronomically crop species, then U. maydis toxins may provide a novel means for biological control of pathogenic fungi.
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Aronson, Arthur I. Function of Bacterial Spore Coat Polypeptides in Structure, Resistance and Germination. Fort Belvoir, VA: Defense Technical Information Center, December 1990. http://dx.doi.org/10.21236/ada232217.

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Zlotkin, Eliahu, Shizuo G. Kamita, Nor Chejanovsky, and S. Maeda. Targeting of an Expressed Insect Selective Neurotoxin by its Recombinant Baculovirus: Pharmacokinetic and Pharmacodynamic Aspects. United States Department of Agriculture, July 1995. http://dx.doi.org/10.32747/1995.7571354.bard.

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Objectives: 1) Clarification of the mode of potentiation of an expressed insect selective neurotoxin (AaIT) by its recombinant baculovirus. 2) In vitro formation and/or modification of neuroactive polypeptides for the design of new improved recombinant baculoviruses. Results: 1) A combined utilization of bioassays, LM-cytochemistry, the highly resolutive EM immunogold and electrical recording from the CNS of baculovirus and AaIT - expressing – recombinant baculovirus infected larvae it has been shown that the recombinant virus potentiates the effect of the toxin. Potentiation is achieved through its continuous expression in the infected tracheal epithelia thus providing a: a) Local supply of freshly produced toxin in the vicinity of its traget sites; b) Translocation of the expressed toxin to the insect CNS. The latter exposes the recombinant toxin to new, critical, target sites which are inaccessible through the natural route of scorpion envenomation. 2) Subjecting a recombinant AaIT toxin to a newly designed system of random mutagenesis results in large numbers of new AaIT genes with amino acid substitutions. The new or modified toxin genes were inserted into a linear BmNPV expressed in silkworm cell culture and assayed on blowfly and silkworm larvae. Thus a system for mass formation and screening of neuroactive agents was developed. Contribution to agriculture: 1) Demonstration of the insecticidal mechanism, capacity and utility of the combination of neuroactive polypeptides and recombinant pathogens. 2) Development of a simple in vitro system for the formation and selection of new neuroactive polypeptides.
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Storrs, R. W. Structural studies of polypeptides: Mechanism of immunoglobin catalysis and helix propagation in hybrid sequence, disulfide containing peptides. Office of Scientific and Technical Information (OSTI), August 1992. http://dx.doi.org/10.2172/6707762.

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Storrs, Richard Wood. Structural studies of polypeptides: Mechanism of immunoglobin catalysis and helix propagation in hybrid sequence, disulfide containing peptides. Office of Scientific and Technical Information (OSTI), August 1992. http://dx.doi.org/10.2172/10131755.

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Yan, John. Functional Separation of Multimodular Type I PKS Polypeptides by Utilizing Matched Docking Domains From a Heterologous PKS System. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.135.

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