Relevant bibliographies by topics / Metal binding sites

Academic literature on the topic 'Metal binding sites'

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Published: 10 March 2023

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Journal articles on the topic "Metal binding sites"

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Tainer, John A., Victoria A. Roberts, and Elizabeth D. Getzoff. "Protein metal-binding sites." Current Biology 2, no. 10 (October 1992): 552. http://dx.doi.org/10.1016/0960-9822(92)90035-9.

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Tainer, John A., Victoria A. Roberts, and Elizabeth D. Getzoff. "Protein metal-binding sites." Current Opinion in Biotechnology 3, no. 4 (August 1992): 378–87. http://dx.doi.org/10.1016/0958-1669(92)90166-g.

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Tainer, John A., Victoria A. Roberts, and Elizabeth D. Getzoff. "Metal-binding sites in proteins." Current Opinion in Biotechnology 2, no. 4 (August 1991): 582–91. http://dx.doi.org/10.1016/0958-1669(91)90084-i.

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Sharma, Ashok, Sudeep Roy, Kumar Parijat Tripathi, Pratibha Roy, Manoj Mishra, Feroz Khan, and Abha Meena. "Predicted metal binding sites for phytoremediation." Bioinformation 4, no. 2 (September 5, 2009): 66–70. http://dx.doi.org/10.6026/97320630004066.

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Lu, Yi, and Joan S. Valentine. "Engineering metal-binding sites in proteins." Current Opinion in Structural Biology 7, no. 4 (August 1997): 495–500. http://dx.doi.org/10.1016/s0959-440x(97)80112-1.

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Regan, Lynne. "Protein design: novel metal-binding sites." Trends in Biochemical Sciences 20, no. 7 (July 1995): 280–85. http://dx.doi.org/10.1016/s0968-0004(00)89044-1.

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Illi, Sarah, Johanna Schulten, and Peter Klüfers. "Metal-binding Sites ofN-Acetylneuraminic Acid." Zeitschrift für anorganische und allgemeine Chemie 639, no. 1 (October 30, 2012): 77–83. http://dx.doi.org/10.1002/zaac.201200415.

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Kökçam-Demir, Ülkü, Anna Goldman, Leili Esrafili, Maniya Gharib, Ali Morsali, Oliver Weingart, and Christoph Janiak. "Coordinatively unsaturated metal sites (open metal sites) in metal–organic frameworks: design and applications." Chemical Society Reviews 49, no. 9 (2020): 2751–98. http://dx.doi.org/10.1039/c9cs00609e.

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The defined synthesis of OMS in MOFs is the basis for targeted functionalization through grafting, the coordination of weakly binding species and increased (supramolecular) interactions with guest molecules.
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Gilg, Kathrin, Tobias Mayer, Natascha Ghaschghaie, and Peter Klüfers. "The metal-binding sites of glycose phosphates." Dalton Transactions, no. 38 (2009): 7934. http://dx.doi.org/10.1039/b909431h.

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Passerini, A., M. Lippi, and P. Frasconi. "Predicting Metal-Binding Sites from Protein Sequence." IEEE/ACM Transactions on Computational Biology and Bioinformatics 9, no. 1 (January 2012): 203–13. http://dx.doi.org/10.1109/tcbb.2011.94.

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Dissertations / Theses on the topic "Metal binding sites"

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Gapian, Bianké Jean-Paul. "DNA mimics containing artificial metal-binding sites /." [S.l.] : [s.n.], 2006. http://www.zb.unibe.ch/download/eldiss/06bianke_g.pdf.

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Torrance, James William. "The geometry and evolution of catalytic sites and metal binding sites." Thesis, University of Cambridge, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.612125.

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Higgins, Sean. "The design of conducting polymers with metal binding sites." Thesis, University of St Andrews, 1998. http://hdl.handle.net/10023/14786.

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This study is concerned with the synthesis of conjugated polyheterocycles with potential metal binding sites for applications in sensors, catalysis and electronics. The first synthetic approach to polyheterocycles was based on the interfacial polycondensation of a dihydrazide derivative of pyridine with a diacid chloride to produce a precursor polymer. It was shown, however, the starting materials could not be easily prepared in high yield. Model studies confirmed the feasibility of the route but these studies also suggested that the precursor polymers were unlikely to be very soluble. The second precursor route explored began with the preparation of 2,6-diethynylpyridine. The intermolecular Glaser coupling of the ethyne groups afforded the precursor polymer, poly((2,6'-pyridyl)but-l,3-diyne), as a black powder which was insufficiently soluble to allow conversion to the poly heterocycles. A series of dimers and trimers containing various combinations of 2-furyl, 2-thienyl and 2-pyridyl moieties were prepared using two different coupling procedures that yielded compounds with the required 2,2'-heteroatom arrangement as required for metal binding. Some of these monomers were electropolymerised and the metal binding properties of these polymers was investigated by cychc voltammetry. In particular, the two trimers: 2,5-di-(2-thienyl) pyridine; and 2,6-di-(2-thienyl) pyridine showed potential metal coordination despite their hydrophobic nature and impermeability towards metal complexes. Evidence was presented to suggest that these polymers are protonated during the electropolymerisation reaction. X-ray analysis of the 2,5-di-(2-thienyl) pyridine showed that only the 2,2'-linked thiophene was coplanar with the pyridine due to a charge transfer interaction. This interaction insures that S and N atoms have a planar syn arrangement conducive to metal binding. Several oligothiophenes were prepared to investigate methods for enhancing the solubility of polyheterocycles. The knowledge gained from these investigations was used to prepare a series of regiochemically well-defined poly((3-alkyl)thiophenes). The regularity of these polymers was confirmed by NMR analysis. Related monomers were prepared containing the necessary solubilising alkyl groups as well as phenyl groups designed to act as acceptor ligands for the low-valent transition metals such as ruthenium(II). The electrochemistry of these novel thiophene monomers is reported.
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Gregory, David St John. "Prediction, design and characterisation of metal binding sites in antibodies." Thesis, University of Oxford, 1992. https://ora.ox.ac.uk/objects/uuid:630ede76-2db6-4e59-bdbe-d337d4fe07a9.

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The design and creation of a functional metalloanti body is presented. A survey of metalloprotein structures was carried out to determine the common structural features of metal binding sites. Metal ligands were then introduced into hypervariable loop 11 of the anti-lysozyme antibody HyHEL-5 and the site comprehensively modelled. The final model was used as a basis for site-directed mutagenesis and mutant antibodies were produced using a Xenopus laevis oocyte expression system. Antigen binding studies showed the mutants to have an affinity for lysozyme equivalent to the parent antibody, while subsequent metal binding experiments have shown the new site to be capable of binding the transition metals cobalt, nickel, copper, zinc and cadmium. A method for the rapid prediction and design of metal binding sites in proteins is described. A protein structure is screened for the location of putative metal sites by template matching. After the introduction of suitable liganding residues, the metal binding potential at each site is evaluated using hydrophobicity contrast. A point representing the metal ion within a new site may be optimised with-respect-to the ligands using multidimensional minimisation. The method has been tested on known metalloprotein structures. It was routinely able to identify the metal binding sites and position a metal point in the site to within 0.6A of the actual metal ion.
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Hannan, Jonathan Paul. "NMR spectroscopic studies of transition metal binding sites in metalloproteins." Thesis, University of East Anglia, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.323296.

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Uppal, Daljit Kaur. "Studies of the metal-binding sites in macrocyclic quadridentate ligands." Thesis, London Metropolitan University, 1986. http://repository.londonmet.ac.uk/3284/.

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Jeong, Chang-Yoon. "Modelling metal competition for adsorption sites on humic acid." Thesis, University of Nottingham, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.389363.

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McMahon, Jennifer Nicole. "Heavy metal competition for acid volatile sulfide binding sites in southeastern coastal sediments." Thesis, Georgia Institute of Technology, 1997. http://hdl.handle.net/1853/19134.

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Yang, Ying. "Mechanism of metal delivery and binding to transport sites of Cu+-transporting ATPases." Link to electronic thesis, 2005. http://www.wpi.edu/Pubs/ETD/Available/etd-042905-112044/.

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Lazarides, Theodore. "Luminescent d-block metal polypyridyl complexes bearing secondary macrocyclic or non-macrocyclic binding sites." Thesis, University of Sheffield, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.427184.

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Books on the topic "Metal binding sites"

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O, Hill H. A., Sadler P. J, and Thompson A. J, eds. Metal sites in proteins and models: Redox centres. Berlin: Springer, 1998.

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Uppal, Daljit Kaur. Studies of the metal-binding sites in macrocyclic quadridentate ligands. 1986.

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H. A. O. Hill (Editor), P. J. Sadler (Editor), and A. J. Thomson (Editor), eds. Metal Sites in Proteins and Models: Redox Centres (Structure and Bonding). Springer-Verlag Telos, 1998.

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G Protein Methods and Protocols (Neuromethods). Humana Press, 1997.

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1947-, Baker Glen B., Boulton A. A, and Mishra Ram K, eds. G protein methods and protocols: Role of G proteins in psychiatric and neurological disorders. Totowa, N.J: Humana Press, 1997.

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Boulton, Alan A., Glen B. Baker, and Ram K. Mishra. G Protein Methods and Protocols: Role of G Proteins in Psychiatric and Neurological Disorders. Humana Press, 2013.

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Book chapters on the topic "Metal binding sites"

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Sun, Hongzhe, Mark C. Cox, Hongyan Li, and Peter J. Sadler. "Rationalisation of metal binding to transferrin: Prediction of metal-protein stability constants." In Metal Sites in Proteins and Models, 71–102. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/3-540-62870-3_3.

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Beer, Paul D., Christopher J. Jones, Jon A. McCleverty, and Sithy S. Salam. "Redox Responsive Metal Complexes Containing Cation Binding Sites." In Inclusion Phenomena in Inorganic, Organic, and Organometallic Hosts, 413–16. Dordrecht: Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-009-3987-5_68.

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Long, Eric C., Paula D. Eason, and Daniel F. Shullenberger. "Incorporation of Square-Planar Metal Binding Sites into Protein Polymeric Structures." In Metal-Containing Polymeric Materials, 481–89. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-0365-7_36.

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Toney, Michael D., Erhard Hohenester, John W. Keller, and Johan N. Jansonius. "Dialkylglycine decarboxylase structure: alkali metal binding sites and bifunctional active site." In Biochemistry of Vitamin B6 and PQQ, 141–45. Basel: Birkhäuser Basel, 1994. http://dx.doi.org/10.1007/978-3-0348-7393-2_23.

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Kotrba, Pavel, Lubomír Rulíšek, and Tomas Ruml. "Bacterial Surface Display Surface display of Metal-Binding Sites." In Microbial Biosorption of Metals, 249–83. Dordrecht: Springer Netherlands, 2011. http://dx.doi.org/10.1007/978-94-007-0443-5_11.

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Grossoehme, Nicholas E., and David P. Giedroc. "Allosteric Coupling Between Transition Metal-Binding Sites in Homooligomeric Metal Sensor Proteins." In Methods in Molecular Biology, 31–51. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-61779-334-9_3.

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Frasch, Wayne D., Michelle Spano, and Russell Lobrutto. "VO2+ as a Probe of Metal Binding Sites in Rubisco Activase." In Photosynthesis: from Light to Biosphere, 4149–52. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-009-0173-5_976.

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Adhikari, Swati, and Parthajit Roy. "A Geometry Based Algorithm for Comparison of Tetrahedral Metal Binding Sites." In Lecture Notes in Networks and Systems, 191–99. Singapore: Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-16-0980-0_19.

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Erat, Michèle C., and Roland K. O. Sigel. "2. Methods to Detect and Characterize Metal Ion Binding Sites in RNA." In Structural and Catalytic Roles of Metal Ions in RNA, 37–100. Cambridge: Royal Society of Chemistry, 2011. http://dx.doi.org/10.1039/9781849732512-00037.

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Baxa, Michael C., and Tobin R. Sosnick. "Engineered Metal-Binding Sites to Probe Protein Folding Transition States: Psi Analysis." In Protein Folding, 31–63. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1716-8_2.

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Conference papers on the topic "Metal binding sites"

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Küçükbay, Serkan, and Hasan Oğul. "Predicting Metal-Binding Sites of Protein Residues." In 2015 Federated Conference on Computer Science and Information Systems. PTI, 2015. http://dx.doi.org/10.15439/2015f391.

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Miller, Yifat. "Preface of the "Symposium on metal binding sites in amyloids"." In INTERNATIONAL CONFERENCE OF COMPUTATIONAL METHODS IN SCIENCES AND ENGINEERING 2014 (ICCMSE 2014). AIP Publishing LLC, 2014. http://dx.doi.org/10.1063/1.4897685.

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BOBADILLA, L., F. NIÑO, and G. NARASIMHAN. "PREDICTING AND CHARACTERIZING METAL-BINDING SITES USING SUPPORT VECTOR MACHINES." In Proceedings of the International Conference. WORLD SCIENTIFIC, 2005. http://dx.doi.org/10.1142/9789812702098_0028.

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Brodsky, G. L., and S. P. Bajaj. "DETERMINATION OF NUMBER OF γ-CARBOXYGLUTAMIC ACID (GLA) RESIDUES INVOLVED IN FORMING THE TWO HIGH AFFINITY METAL BINDING SITES IN PROTHROMBIN AND FACTOR X." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643934.

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Prothrombin and factor X possess two high affinity and several low affinity lanthanide ion binding sites. In both proteins, the association constant of the high affinity sites is at least 50-fold greater than that of the low affinity sites. Moreover, metal bound to these high affinity sites is extremely difficult to displace. It has been proposed that one of the two high affinity sites in factor X involves Gla residues while the other involves β-hydroxyaspartic acid and no Gla residues. It is also known that ^H can be specifically incorporated into Gla residues at an acidic pH. We have determined that under nondenaturing conditions when Gla (synthetic or in proteins) is complexed to metal at pH 5.5, this specific 3H incorporation is blocked. Furthermore, we have found that β-hydroxyaspartic acid does not incorporate in the presence or absence of metal. When we incubated prothrombin or factor X (41 μM) with 3H2O in the presence of Tb3+ or Gd3+ (82 μM), we blocked 5.6 Gla residues per prothrombin and 5.5 Gla residues per factor X from 3H incorporation. Under these conditions, we calculated that >95% of the high affinity sites are occupied by metal. Thus, in prothrombin, an average of 2.8 Gla residues are involved in forming each high affinity site. If the Gla residues in factor X participate in forming only one of the two high affinity sites, then all 5.5 Gla residues blocked from incorporation must be involved in forming that site. However, this seems highly unlikely. We conclude that, as in prothrombin, both high affinity sites in factor X involve Gla residues (average 2.75/site). However, our data does not exclude the possibility of existence of a heterologous site containing both β-hydroxyaspartic acid and Gla residues.
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Wong, Eric K. L., and Geraldine L. Richmond. "Laser excitation spectroscopy: a probe of metal ion binding in polymers." In International Laser Science Conference. Washington, D.C.: Optica Publishing Group, 1986. http://dx.doi.org/10.1364/ils.1986.fg6.

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The structure and the function of many macromolecules and organic polymers are dependent on the specific sites bound to metal ions. Metal binding in some ionic polymers is in the form of ionic clusters. The objective of our laser-induced fluorescence studies is to gain a better understanding of the structure and binding properties of these clusters by using europium ions as probes. Eu(III) has many unique spectral properties which make it a good luminescent probe of the metal binding in polymers. The energy, fluorescence quantum yield, and lifetime of the excited state of the 7F0 → 5D0 transition near 580 nm are very sensitive to the environment of the ions. By studying this transition in detail, it is possible to obtain unique optical information about the metal–molecule interaction. Metal binding in the perfluorosulfonate membrane, Nation (DuPont), has been studied here as function of such parameters as metal ion concentration and pH. The resulting excitation spectra show multiple peaks corresponding to different ionic environments. The results of these experiments are discussed in terms of the known macroscopic binding properties of this film.
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Sugo, T., S. Tanabe, K. Shinoda, and M. Matsuda. "MONOCLONAL ANTIBODIES THAT RECOGNIZE Ca2+-INDUCED CONFORMER OF PROTEIN C, INDEPENDENT OF GLA RESIDUES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643644.

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Monoclonal antibodies (MCA’s) were prepared against human protein C (PC) according to Köhler & Milstein, and those that recognize the Ca2+-dependent PC conformers were screened by direct ELISA in the presence of 2 mM either CaCl2 or EDTA. Out of nine MCAߣs thus screened, five MCA's designated as HPC-1˜5, respectively, were found to react with PC in the presence of Ca2+ but not EDTA. By SDS-PAGE coupled with Western Blotting performed in the presence of 2 mM CaCl2, we found that two MCA’s HPC-1 and 2, recognized the light chain, and two others, HPC-3 and 4, recognized the heavy chain of PC. But another MCA, HPC-5 was found to react with only non-reduced antigens. Further study showed that HPC-1 and 5 failed to react with the Gla-domainless PC, i.e. PC from which the N-terminal Gla-domain of the light chain had been cleaved off by α-chymotrypsin. However, all the other three MCA's retained the reactivity with the antigen in the presence of Ca2+ even after the Gla-domain had been removed. The binding of these MCA’s to PC in the presence of Ca2+ was found to be saturable with respect to the Ca2+ concentration and the half maximal binding for each MCA was calculated to be about 0.5+mM. Moreover, many other divalent cations such as Mg2+, Mn2+ , Ba2+, Zn2+, Co2+, Sr2+, were found to substitute for Ca2+ in inducing the metal ion-dependent but Gla-domain-independent conformer of PC.Cross-reactivity to other vitamin K-aependent plasma proteins was examined by direct ELISA; HPC-2 and 3 reacted solely to PC, but HPC-1 and 4 also reacted with prothrombin and HPC-5 with both prothrombin and factor X.These findings indicated that there are two or more metal binding sites besides the Gla-domain, possibly one in the light chain and the other(s) in the heavy chain. The presence of these metal binding sites may contribute to the unique conformer of vitamin K-dependent plasma proteins including protein C.
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Higashiyama, S., I. Ohkubo, H. Ishiguro, and M. Sasaki. "A NEW FUNCTION OF HUMAN KININOGENS: THE AMINO-TERMINAL REGION OF DOMAIN 1 INVOLVES AN EF HAND-LIKE STRACTURE FOR METAL BINDING." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642851.

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Two types of kininogens in mammalian plasma, high molecular weight (HMW) and low molecular weight (LMW) kininogens, are the precursors of kinin. Especially, HMW kininogen circulates in the plasma as a complex with prekallikrein and factor XI, and functions as a cofactor in the initial phase reactions of intrinsic blood coagulation cascade. Recently, it has been found that the kininogens have inhibitory activity toward cysteine proteinases. The heavy chain portion, which is identical for HMW and LMW kininogens, is composed of three domains, domain 1, 2 and 3. Each the domain 2 and 3 has a reactive site as a cysteine proteinase inhibitor. However, physiological function of domain 1 remains still unknown. By using the antibody recognizing the interaction between HMW kininogen and Ca2+ (anti-HMW kininogen-Ca2+ antibody) as a probe, we newly found the Ca2+ binding site in the domain 1.Anti-HMW kininogen-Ca2+ antibody was isolated from anti-HMW kininogen antiserum as an antibody which bound to a HMW kininogen-Sepharose column equilibrated with 40 mM Tris-HCl buffer, pH 7.5, containing 1.0 M NaCl and 1 mM CaCl2, and was eluted with 3 mM EDTA. Resulting from the characterization by ELISA, this antibody specifically recognized the CB-1 region (CNBr-cleavage fragment 1: 1-160 amino acid sequence) of the heavy chain of kininogen molecules in the presence of Ca2+ or Mg2+. Furthermore, circular dichroism (CD) experiments showed that the conformational changes of HMW kininogen and heavy chain were induced by the addition of metal ions such as Ca2+ or Mg2+, and that this change was due to the conformational change of the CB-1 region. The dissociation constant (Kd) for heavy chain measured by Ca2+ titration analysis by CD at 214 nm was found to be 0.33 ± 0.09 mM. The number of Ca2+ binding sites of heavy chain calculated from Hill plot was 1.15 ± 0.04. The EF handlike structure found in the amino-terminal portion of the heavy chain of kininogen molecules strongly supported the above data. This indicates a possibility that kininogens play an important role as a Ca2+ binding protein.
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KÖhlin, A., and J. Stenflo. "HIGH AFFINITY CALCIUM BINDING TO DOMAINES OF PROTEIN C THAT ARE HOMOLOGUS TO THE EPIDERMAL GROWTH FACTOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643645.

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In addition to γ-carboxyglutamic acid (Gla)-dependent calcium binding all of the vitamin K-dependent plasma proteins, except prothrombin, have one or two high affinity calcium binding sites that do not require the Gla residues. A common denominator among these proteins (factors IX, X, protein C, protein Z and protein S) is that they have domaines that are homologus to the epidermal growth factor (EGF) precursor. In factors VII,IX,X, protein C and in protein Z the aminoterminal of two EGF homology regions contain one residue of β-hydroxyaspartic acid (Hya) whereas in protein S the aminoterminal EGF homology region contains Hya and the three following contain one β-hydroxyasparagine residue each.In an attempt to elucidate the role of the EGF homology regions in the Gla independent calcium binding we have isolated a tryptic fragment (residue 44-138) from the light chain of human protein C. The fragment was isolated using a monoclonal antibody that recognizes a calcium ion stabilized epitope that is expressed both in intact protein C and in protein C lacking the Gla domaine.The antibody bound the isolated EGF homology region in the presence of calcium ions but not in EDTA containing buffer. A calcium ion titration showed half maximal binding at approximately 200 μM Ca2+. The metal ion induced conformational change in the isolated fragment was also studied with affinity purified rabbit antibodies against Gla domainless protein C. Antibodies that bound in the presence of calcium ions and that could be eluted with EDTA recognized the metal ion induced conformational change in the isolated EGF homology domain. Our results suggest that one or both of the EGF homology regions are involved in the Gla-independent high affinity calcium binding in the vitamin K-dependent plasma proteins.
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Kaufman, Randal J., Debra D. Pittman, Louise C. Wasley, W. Barry Foster, Godfrey W. Amphlett, and Alan R. Giles. "DIRECTED MUTAGENESIS IN THE STUDY OF THE REQUIREMENTS FOR FACTOR VIII ACTIVITY IN VITRO AND IN VIVO." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644769.

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Factor VIII is a high molecular weight plasma glycoprotein that functions in the blood clotting cascade as the cofactor for factor DCa proteolytic activation of factor X. Factor VIII does not function proteolytically in this reaction hut itself can be proteolytically activated by other coagulation enzymes such as factor Xa and thrombin. In the plasma, factor VIII exists as a 200 kDa amino-terminal fragment in a metal ion stabilized complex with a 76 kDa carboxy-terminal fragment. The isolation of the cENA for human factor VIII provided the deduced primary amino acid sequence of factor VIIT and revealed three distinct structural domains: 1) a triplicated A domain of 330 amino acids which has homology to ceruloplasmin, a plasma copper binding protein, 2) a duplicated C domain of 150 amino acids, and 3) a unique B domain of 980 amino acids. These domains are arranged as shown below. We have previously reported the B domain is dispensible far cofactor activity in vitro (Toole et al. 1986 Proc. Natl. Acad 5939). The in vivo efficacy of factor VIII molecules harboring the B domain deletion was tested by purification of the wildtype and modified forms and infusion into factor VIII deficient, hemophilic, dogs. The wildtype and the deleted forms of recombinant derived factor VIII exhibited very similar survival curves (Tl/2 = 13 hrs) and the cuticle bleeding times suggested that both preparations appeared functionally equivalent. Sepharose 4B chromatography indicated that both factor VIII molecules were capable of binding canine plasma vWF.Further studies have addressed what cleavages are necessary for activation of factor VIII. The position of the thrombin, factor Xa, and activated protein C (AFC) cleavage sites within factor VIII are presented below, site-directed ENA medicated mutagenesis has been performed to modify the arginine at the amino side of each cleavagesite to an soleucine. In all cases this modification resulted in molecules that were resistant to cleavage by thrombin at the modified site. Modification of the thrombin cleavage sites at 336 and 740 and modification of the factor Xa cleavage site at 1721 resulted in no loss of cofactor activity. Modification of the thrombin cleavage site at either 372 or 1689 destroyed oofactor activity. Modification of the thrombin cleavage site at 336 resulted in a factor VIII having an increased activity, possibly due to resistance to inactivation. These results suggest the requirement of cleavage at residues 372 and 1689 for cofactor activity.
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Liu, Zilong, Hayati Onay, Fengzhi Guo, and Pegah Hedayati. "Electrochemically Assisted Deposition of Calcium Carbonate Surfaces for Anionic Surfactant Adsorption: Implications for Enhanced Oil Recovery." In SPE International Conference on Oilfield Chemistry. SPE, 2021. http://dx.doi.org/10.2118/204283-ms.

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Abstract Surface roughness of rocks had a significant influence on surfactant adsorption in enhanced oil recovery (EOR), both in terms of the total amount adsorbed as well as of the kinetics of adsorption. Combining electrochemical techniques and quartz crystal microbalance with dissipation monitoring (QCM) into one analysis setup opens up new avenues for depositing model rock surfaces and investigating the adsorption behavior. Using electrochemically assisted deposition, uniform and well-covered metal-CaCO3 sensors were obtained to simulate rough carbonate rocks and characterized by scanning electron microscope with energy dispersive X-ray analysis (SEM-EDX). The deposition process was controlled by the nitrate and oxygen electroreduction reactions in the presence of bicarbonate and calcium ions. The deposited mass of CaCO3 was calculated and the coverages for Au-CaCO3 and Pt-CaCO3 sensors were between 20 - 60%. It is observed that mostly cubic-like CaCO3 crystals were formed with crystal sizes around 20 to 50 µm from the SEM micrographs. The bigger crystals were surrounded by bare regions of Pt surface, suggesting the existence of Ostwald ripening process. Prior to the investigation of the deposited CaCO3 surfaces, the adsorption of anionic surfactant alcohol alkoxy sulfate (AAS) was studied on a smooth commercial CaCO3 surface with varying pH and CaCl2concentrations using QCM. Subsequently, surfactant adsorption was performed on the rough deposited CaCO3 surfaces and their adsorption behavior were compared. On a smooth CaCO3 surface, a fast adsorption of AAS surfactant was observed, whereas the desorption process was characterized as a two-step process. Compared to the smooth CaCO3surface, an increase of the frequency shift of about 5 times was observed on the deposited CaCO3 surfaces. This observation was mainly ascribed to the rougher surfaces, having more adsorption sites for AAS binding, and also the liquid trapping effect, resulting in more frequency shifts. It is suggested that a rough model mineral surface could be a better representation of a rock surface, presenting the implications of the new understanding for surfactant adsorption on different rock surfaces in EOR.
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Reports on the topic "Metal binding sites"

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Borovik, A. S. Metallo-Network Polymers: Biomimetic Metal Binding/Recognition Sites. Fort Belvoir, VA: Defense Technical Information Center, October 2000. http://dx.doi.org/10.21236/ada383458.

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Hodges, Thomas K., and David Gidoni. Regulated Expression of Yeast FLP Recombinase in Plant Cells. United States Department of Agriculture, September 2000. http://dx.doi.org/10.32747/2000.7574341.bard.

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Research activities in both our laboratories were directed toward development of control of the FLP/frt recombination system for plants. As described in the text of the research proposal, the US lab has been engaged in developing regulatory strategies such as tissue-specific promoters and the steroid-inducible activation of the FLP enzyme while the main research activities in Israel have been directed toward the development and testing of a copper-regulated expression of flp recombinase in tobacco (this is an example of a promoter activation by metal ions). The Israeli lab hat additionally completed experiments of previous studies regarding factors affecting the efficiency of recombinase activity using both a gain-of-function assay (excisional-activation of a gusA marker) and loss of function assay (excision of a rolC marker) in tobacco. Site-specific recombinase systems, in particular the FLP/frt and R/RS systems of yeast and the Cre/lox system of bacteriophage P1, have become an essential component of targeted genetic transformation procedures both in animal and plant organisms. To provide more flexibility in transgene excisions by the recombinase systems as well as gene targeting, and to widen possible applications, the development of controlled or regulated recombination systems is highly desirable and was therefore the subject of this research proposal. There are a few possible mechanisms to regulate expression of a recombinase system. They include: 1) control of the recombination system by having the target sites (e.g. frt) in one plant and the flp recombinase gene in another, and bringing the two together by cross fertilization. 2) regulation of promoter activities by external stimuli such as temperature, chemicals, metal ions, etc. 3) regulation of promoter activities by internal signals, i.e. cell- or tissue-specific, or developmental regulation. 4) regulation of enzyme activity by providing cofactors essential for biochemical reactions to take place such as steroid molecules in conjunction with a steroid ligand-binding protein (domains). During the course of this research our major emphasis have been focused toward studying the feasibility of hybrid seed production in Arabidopsis, using FLP/frt. Male-sterility was induced using the antisence of a pollen- and tapetum-specific gene, bcp1, isolated from Arabidopsis. The sterility inducing gene was flanked by frt sites. Upon cross pollination of flowers of male-sterile plants with pollen from FLP-containing plants, viable seeds were produced, and the progeny hybrid plants developed normally. The major achievement from this work is the first demonstration of using a site-specific recombinase to restore fertility in male-sterile plants (see attached paper, Luo et al., Plant J 2000; 23:423-430). The implication from this finding is that site-specific recombination systems can be applied in crop plants as a useful alternative method for hybrid seed production.
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Rahimipour, Shai, and David Donovan. Renewable, long-term, antimicrobial surface treatments through dopamine-mediated binding of peptidoglycan hydrolases. United States Department of Agriculture, January 2012. http://dx.doi.org/10.32747/2012.7597930.bard.

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There is a need for renewable antimicrobial surface treatments that are semi- permanent, can eradicate both biofilms and planktonic pathogens over long periods of time and that do not select for resistant strains. This proposal describes a dopamine binding technology that is inexpensive, bio-friendly, non-toxic, and uses straight-forward commercially available products. The antimicrobial agents are peptidoglycanhydrolase enzymes that are non-toxic and highly refractory to resistance development. The goal of this project is to create a treatment that will be applicable to a wide variety of surfaces and will convey long-lasting antimicrobial activity. Although the immediate goal is to create staphylolytic surfaces, the technology should be applicable to any pathogen and will thus contribute to no less than 3 BARD priorities: 1) increased animal production by protecting animals from invasive and emerging diseases, 2) Antimicrobial food packaging will improve food safety and security and 3) sustainable bio- energy systems will be supported by coating fermentation vats with antimicrobials that could protect ethanolic fermentations from Lactobacillus contamination that reduces ethanol yields. The dopamine-based modification of surfaces is inspired by the strong adhesion of mussel adhesion proteins to virtually all types of surfaces, including metals, polymers, and inorganic materials. Peptidoglycanhydrolases (PGHs) meet the criteria of a surface bound antimicrobial with their site of action being extracellular peptidoglycan (the structural basis of the bacterial cell wall) that when breached causes osmotic lysis. As a proof of principle, we will develop technology using peptidoglycanhydrolase enzymes that target Staphylococcus aureus, a notoriously contagious and antimicrobial-resistant pathogen. We will test for susceptibility of the coating to a variety of environmental stresses including UV light, abrasive cleaning and dessication. In order to avoid resistance development, we intend to use three unique, synergistic, simultaneous staphylococcal enzyme activities. The hydrolases are modular such that we have created fusion proteins with three lytic activities that are highly refractory to resistance development. It is essential to use multiple simultaneous activities to avoid selecting for antimicrobial resistant strains. This strategy is applicable to both Gram positive and negative pathogens. We anticipate that upon completion of this award the technology will be available for commercialization within the time required to achieve a suitable high volume production scheme for the required enzymes (~1-2 years). We expect the modified surface will remain antimicrobial for several days, and when necessary, the protocol for renewal of the surface will be easily applied in a diverse array of environments, from food processing plants to barnyards.
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