Relevant bibliographies by topics / Binding sites (Biochemistry) Ligand binding (Biochemistry)

Academic literature on the topic 'Binding sites (Biochemistry) Ligand binding (Biochemistry)'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Contents

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Binding sites (Biochemistry) Ligand binding (Biochemistry).'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Binding sites (Biochemistry) Ligand binding (Biochemistry)"

1

Vidad, Ashley Ryan, Stephen Macaspac, and Ho Leung Ng. "Locating ligand binding sites in G-protein coupled receptors using combined information from docking and sequence conservation." PeerJ 9 (September 24, 2021): e12219. http://dx.doi.org/10.7717/peerj.12219.

Full text
Abstract:
GPCRs (G-protein coupled receptors) are the largest family of drug targets and share a conserved structure. Binding sites are unknown for many important GPCR ligands due to the difficulties of GPCR recombinant expression, biochemistry, and crystallography. We describe our approach, ConDockSite, for predicting ligand binding sites in class A GPCRs using combined information from surface conservation and docking, starting from crystal structures or homology models. We demonstrate the effectiveness of ConDockSite on crystallized class A GPCRs such as the beta2 adrenergic and A2A adenosine receptors. We also demonstrate that ConDockSite successfully predicts ligand binding sites from high-quality homology models. Finally, we apply ConDockSite to predict the ligand binding sites on a structurally uncharacterized GPCR, GPER, the G-protein coupled estrogen receptor. Most of the sites predicted by ConDockSite match those found in other independent modeling studies. ConDockSite predicts that four ligands bind to a common location on GPER at a site deep in the receptor cleft. Incorporating sequence conservation information in ConDockSite overcomes errors introduced from physics-based scoring functions and homology modeling.
APA, Harvard, Vancouver, ISO, and other styles
2

Whittaker, Linda, Caili Hao, Wen Fu, and Jonathan Whittaker. "High-Affinity Insulin Binding: Insulin Interacts with Two Receptor Ligand Binding Sites†." Biochemistry 47, no. 48 (December 2, 2008): 12900–12909. http://dx.doi.org/10.1021/bi801693h.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Linthicum, D. S., M. B. Bolger, P. H. Kussie, G. M. Albright, T. A. Linton, S. Combs, and D. Marchetti. "Analysis of idiotypic and anti-idiotypic antibodies as models of receptor and ligand." Clinical Chemistry 34, no. 9 (September 1, 1988): 1676–80. http://dx.doi.org/10.1093/clinchem/34.9.1676.

Full text
Abstract:
Abstract Antibodies to small bioactive ligands and peptides may mimic the binding characteristics of the natural receptor; in turn, the anti-idiotypic antibodies generated against the binding sites of such anti-ligand antibodies may mimic some aspects of small bioactive ligands and peptides. Among the several levels of investigation of such antibody-receptor networks are (a) the quantitative structure-activity relationships of ligand binding to antibody as compared with natural receptor; (b) the molecular modeling of antibody-receptor binding sites and the genomic basis for such structures; and (c) the characteristics of the molecular mimicry exhibited by "mimetopes" on anti-idiotypic antibodies. To illustrate the analysis encountered at each of these levels, we discuss here antibody and anti-idiotypic systems that are directed to small neuroactive ligands and their receptors.
APA, Harvard, Vancouver, ISO, and other styles
4

Lummis, Sarah C. R. "Locating GABA in GABA receptor binding sites." Biochemical Society Transactions 37, no. 6 (November 19, 2009): 1343–46. http://dx.doi.org/10.1042/bst0371343.

Full text
Abstract:
The Cys-loop family of ligand-gated ion channels contains both vertebrate and invertebrate members that are activated by GABA (γ-aminobutyric acid). Many of the residues that are critical for ligand binding have been identified in vertebrate GABAA and GABAC receptors, and specific interactions between GABA and some of these residues have been determined. In the present paper, I show how a cation–π interaction for one of the binding site residues has allowed the production of models of GABA docked into the binding site, and these orientations are supported by mutagenesis and functional data. Surprisingly, however, the residue that forms the cation–π interaction is not conserved, suggesting that GABA occupies subtly different locations even in such closely related receptors.
APA, Harvard, Vancouver, ISO, and other styles
5

Lin, Win, Michael P. Bernard, Donghui Cao, Rebecca V. Myers, John E. Kerrigan, and William R. Moyle. "Follitropin receptors contain cryptic ligand binding sites." Molecular and Cellular Endocrinology 260-262 (January 2007): 83–92. http://dx.doi.org/10.1016/j.mce.2006.06.012.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Tozer, Eileen Collins, Paul E. Hughes, and Joseph C. Loftus. "Ligand binding and affinity modulation of integrins." Biochemistry and Cell Biology 74, no. 6 (December 1, 1996): 785–98. http://dx.doi.org/10.1139/o96-085.

Full text
Abstract:
Integrins are cell adhesion receptors that mediate cell–cell and cell–extracellular matrix interactions. The extracellular domains of these receptors possess binding sites for a diverse range of protein ligands. Ligand binding is divalent cation dependent and involves well-defined motifs in the ligand. Integrins can dynamically regulate their affinity for ligands (inside-out signaling). This ability to rapidly modulate their affinity state is key to their involvement in such processes as cell migration and platelet aggregation. This review will focus on two aspects of integrin function: first, on the molecular basis of ligand–integrin interactions and, second, on the underlying mechanisms controlling the affinity state of integrins for their ligands.Key words: integrins, ligand binding, affinity modulation.
APA, Harvard, Vancouver, ISO, and other styles
7

Wang, Shiwei, Haoyu Lin, Zhixian Huang, Yufeng He, Xiaobing Deng, Youjun Xu, Jianfeng Pei, and Luhua Lai. "CavitySpace: A Database of Potential Ligand Binding Sites in the Human Proteome." Biomolecules 12, no. 7 (July 11, 2022): 967. http://dx.doi.org/10.3390/biom12070967.

Full text
Abstract:
Location and properties of ligand binding sites provide important information to uncover protein functions and to direct structure-based drug design approaches. However, as binding site detection depends on the three-dimensional (3D) structural data of proteins, functional analysis based on protein ligand binding sites is formidable for proteins without structural information. Recent developments in protein structure prediction and the 3D structures built by AlphaFold provide an unprecedented opportunity for analyzing ligand binding sites in human proteins. Here, we constructed the CavitySpace database, the first pocket library for all the proteins in the human proteome, using a widely-applied ligand binding site detection program CAVITY. Our analysis showed that known ligand binding sites could be well recovered. We grouped the predicted binding sites according to their similarity which can be used in protein function prediction and drug repurposing studies. Novel binding sites in highly reliable predicted structure regions provide new opportunities for drug discovery. Our CavitySpace is freely available and provides a valuable tool for drug discovery and protein function studies.
APA, Harvard, Vancouver, ISO, and other styles
8

Gold, N. D., K. Deville, and R. M. Jackson. "New opportunities for protease ligand-binding site comparisons using SitesBase." Biochemical Society Transactions 35, no. 3 (May 22, 2007): 561–65. http://dx.doi.org/10.1042/bst0350561.

Full text
Abstract:
The rapid expansion of structural information for protein ligand-binding sites is potentially an important source of information in structure-based drug design and in understanding ligand cross-reactivity and toxicity. We have developed SitesBase, a comprehensive database of ligand-binding sites extracted automatically from the Macromolecular Structure Database. SitesBase is an easily accessible database which is simple to use and holds pre-calculated information about structural similarities between known ligand-binding sites. These similarities are presented to the wider community enabling binding-site comparisons for therapeutically interesting protein families, such as the proteases and for new proteins to enable the discovery of interesting new structure–function relationships. The database is available from http://www.modelling.leeds.ac.uk/sb/.
APA, Harvard, Vancouver, ISO, and other styles
9

Puzon-McLaughlin, Wilma, Tetsuji Kamata, and Yoshikazu Takada. "Multiple Discontinuous Ligand-mimetic Antibody Binding Sites Define a Ligand Binding Pocket in Integrin αIIbβ3." Journal of Biological Chemistry 275, no. 11 (March 10, 2000): 7795–802. http://dx.doi.org/10.1074/jbc.275.11.7795.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Anand, Praveen, Deepesh Nagarajan, Sumanta Mukherjee, and Nagasuma Chandra. "ABS–Scan: In silico alanine scanning mutagenesis for binding site residues in protein–ligand complex." F1000Research 3 (September 9, 2014): 214. http://dx.doi.org/10.12688/f1000research.5165.1.

Full text
Abstract:
Most physiological processes in living systems are fundamentally regulated by protein–ligand interactions. Understanding the process of ligand recognition by proteins is a vital activity in molecular biology and biochemistry. It is well known that the residues present at the binding site of the protein form pockets that provide a conducive environment for recognition of specific ligands. In many cases, the boundaries of these sites are not well defined. Here, we provide a web-server to systematically evaluate important residues in the binding site of the protein that contribute towards the ligand recognition through in silico alanine-scanning mutagenesis experiments. Each of the residues present at the binding site is computationally mutated to alanine. The ligand interaction energy is computed for each mutant and the corresponding ΔΔG values are computed by comparing it to the wild type protein, thus evaluating individual residue contributions towards ligand interaction. The server will thus provide clues to researchers about residues to obtain loss-of-function mutations and to understand drug resistant mutations. This web-tool can be freely accessed through the following address: http://proline.biochem.iisc.ernet.in/abscan/.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "Binding sites (Biochemistry) Ligand binding (Biochemistry)"

1

Olsen, Gregory L. "Magnetic resonance studies of binding site structure and dynamics in TAR RNA /." Thesis, Connect to this title online; UW restricted, 2007. http://hdl.handle.net/1773/8581.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Hauser, Melanie R. "Selective calcium binding by alpha-hydoxyketones and alpha-hydroxyamides /." view abstract or download file of text, 2006. http://proquest.umi.com/pqdweb?did=1251854561&sid=3&Fmt=2&clientId=11238&RQT=309&VName=PQD.

Full text
Abstract:
Thesis (Ph. D.)--University of Oregon, 2006.
Typescript. Includes vita and abstract. Includes bibliographical references (leaves 115 - 121). Also available for download via the World Wide Web; free to University of Oregon users.
APA, Harvard, Vancouver, ISO, and other styles
3

Prasannan, Charulata Bhaskaran. "Modulation of restriction enzyme PvuII activity by metal ion cofactors." Diss., St. Louis, Mo. : University of Missouri--St. Louis, 2009. http://etd.umsl.edu/r4461.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Penkler, David Lawrence. "In silico analysis of human Hsp90 for the identification of novel anti-cancer drug target sites and natural compound inhibitors." Thesis, Rhodes University, 2015. http://hdl.handle.net/10962/d1018938.

Full text
Abstract:
The 90-KDa heat shock protein (Hsp90) is part of the molecular chaperone family, and as such it is involved in the regulation of protein homeostasis within cells. Specifically, Hsp90 aids in the folding of nascent proteins and re-folding of denatured proteins. It also plays an important role in the prevention of protein aggregation. Hsp90’s functionality is attributed to its several staged, multi-conformational ATPase cycle, in which associated client proteins are bound and released. Hsp90 is known to be associated with a wide array of client proteins, some of which are thought to be involved in multiple oncogenic processes. Indeed Hsp90 is known to be directly involved in perpetuating the stability and function of multiple mutated, chimeric and over-expressed signalling proteins that are known to promote the growth and survival of cancer cells. Hsp90 inhibitors are thus thought to be promising therapeutic agents for cancer treatment. A lack of a 3D structure of human Hsp90 however has restricted Hsp90 inhibitor development in large to in vivo investigations. This study, aims to investigate and calculate hypothetical homology models of the full human Hsp90 protein, and to probe these structural models for novel drug target sites using several in silico techniques. A multi-template homology modelling methodology was developed and in conjunction with protein-protein docking techniques, two functionally important human Hsp90 structural models were calculated; the nucleotide free “v-like” open and nucleotide bound closed conformations. Based on the conservation of ligand binding, virtual screening experiments conducted on both models using 316 natural compounds indigenous to South Africa, revealed three novel putative target sites. Two binding pockets in close association with important Hsp90-Hop interaction residues and a single binding pocket on the dimerization interface in the C-terminal domain. Targeted molecular docking experiments at these sites revealed two compounds (721395-11-5 and 264624-39-7) as putative inhibitors, both showing strong binding affinities for at least one of the three investigated target sites. Furthermore both compounds were found to only violate one Lipinski’s rules, suggesting their potential as candidates for further drug development. The combined work described here provides a putative platform for the development of next generation inhibitors of human Hsp90.
APA, Harvard, Vancouver, ISO, and other styles
5

Carlsson, Jens. "Challenges in Computational Biochemistry: Solvation and Ligand Binding." Doctoral thesis, Uppsala University, Department of Cell and Molecular Biology, 2008. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-8738.

Full text
Abstract:

Accurate calculations of free energies for molecular association and solvation are important for the understanding of biochemical processes, and are useful in many pharmaceutical applications. In this thesis, molecular dynamics (MD) simulations are used to calculate thermodynamic properties for solvation and ligand binding.

The thermodynamic integration technique is used to calculate pKa values for three aspartic acid residues in two different proteins. MD simulations are carried out in explicit and Generalized-Born continuum solvent. The calculated pKa values are in qualitative agreement with experiment in both cases. A combination of MD simulations and a continuum electrostatics method is applied to examine pKa shifts in wild-type and mutant epoxide hydrolase. The calculated pKa values support a model that can explain some of the pH dependent properties of this enzyme.

Development of the linear interaction energy (LIE) method for calculating solvation and binding free energies is presented. A new model for estimating the electrostatic term in the LIE method is derived and is shown to reproduce experimental free energies of hydration. An LIE method based on a continuum solvent representation is also developed and it is shown to reproduce binding free energies for inhibitors of a malaria enzyme. The possibility of using a combination of docking, MD and the LIE method to predict binding affinities for large datasets of ligands is also investigated. Good agreement with experiment is found for a set of non-nucleoside inhibitors of HIV-1 reverse transcriptase.

Approaches for decomposing solvation and binding free energies into enthalpic and entropic components are also examined. Methods for calculating the translational and rotational binding entropies for a ligand are presented. The possibility to calculate ion hydration free energies and entropies for alkali metal ions by using rigorous free energy techniques is also investigated and the results agree well with experimental data.

APA, Harvard, Vancouver, ISO, and other styles
6

Ridd, Thomas Ian. "Reactions and ligand binding properties of cytochrome P450." Thesis, University of Surrey, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.308553.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Jones, Marc. "Folate binding protein : partial characterisation of bovine milk folate binding protein, includings its ligand binding /." [St. Lucia, Qld], 2004. http://www.library.uq.edu.au/pdfserve.php?image=thesisabs/absthe18263.pdf.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Jiang, Tao. "Characterisation of recombinant aryl hydrocarbon receptor ligand binding domain." Thesis, University of Nottingham, 2004. http://eprints.nottingham.ac.uk/10401/.

Full text
Abstract:
Aryl hydrocarbon receptor (AhR) is a ligand-activated transcription factor, which mediates the toxicity of dioxin and related compounds, and has an important role in development. However, a structural basis for ligand binding to the AhR remains unclear and the study was hindered by the low abundance and inherited instability of the AhR. Based on a previously defined minimal ligand-binding domain (LBD, residues 230-421), in the present study a series of truncated LBD constructs were created and expressed in insect cells (Sf9) using a baculovirus expression system. An antibody was produced to analyze the expressed. The antisera can detect as low as 0.3ng of AhR LBD from cytosol of Sf9. An in vitro [3H]TCDD binding assay was developed to characterized the expressed LBD. The assay yielded an estimate for the KD of C57Bl/6 mouse liver binding at 1.4nM. The present expression system yields soluble AhR LBD protein at ~0.15% of cytosol protein. Supplementation of the Sf9 culture medium with additional glucose resulted in an increase in the amount of soluble AhR, due to an increase in intracellular ATP level. However, cotransfection of LBD with hsp90 interaction protein p23 made no substantial change in the amount of cytosolic AhR. The soluble recombinant LBD retains functionality in the form of specific binding to dioxin, and its thermal stability was indistinguishable from that of mouse liver. However the ligand-binding activity of LBD was molybdate dependent, indicating a weaker association of mouse AhR LBD with Sf9 hsp90. A differential effect of Triton X-100 on the recombinant AhR LBD and native AhR also suggests that the interaction between AhR and Sf9 hsp90 is less stable. The study refined the minimal LBD to a region of 125 amino acids, which should be amenable for structural studies of the LBD.
APA, Harvard, Vancouver, ISO, and other styles
9

Ayre, Elizabeth Anne. "The characterization, localization and physiological regulation of [125I] iodomelatonin binding sites in the gonads." Thesis, [Hong Kong : University of Hong Kong], 1993. http://sunzi.lib.hku.hk/hkuto/record.jsp?B13554177.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

McFail-Isom, Lori. "Effects of ligand binding, coordinate error and ion binding on nucleic acid structure and conformation." Diss., Georgia Institute of Technology, 1998. http://hdl.handle.net/1853/30735.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Books on the topic "Binding sites (Biochemistry) Ligand binding (Biochemistry)"

1

Woodbury, Charles P. Introduction to macromolecular binding equilibria. Boca Raton: CRC Press, 2008.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
2

Thermodynamic theory of site-specific binding processes in biological macromolecules. Cambridge, [Eng.]: Cambridge University Press, 1995.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
3

T, Peters, and Evans S. V. 1959-, eds. Bioactive conformation. Berlin: Springer, 2007.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
4

Cell surface receptors: A short course on theory & methods. 3rd ed. New York: Springer, 2004.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
5

H, Sawyer William, ed. Quantitative characterization of ligand binding. New York: Wiley-Liss, 1995.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
6

Cell surface receptors: A short course on theory and methods. Boston: Nijhoff, 1986.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
7

Limbird, Lee E. Cell surface receptors: A short course on theory and methods. 2nd ed. Boston: Kluwer Academic Publishers, 1996.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
8

William, Hutchens T., J.T. Baker Chemical Co., and University of California, Los Angeles., eds. Protein recognition of immobilized ligands: Proceedings of a J.T. Baker-UCLA Colloquium, held at Santa Fe, New Mexico, December 2-7, 1987. New York: A.R. Liss, 1989.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
9

Wyman, Jeffries. Binding and linkage: Functional chemistry of biological macromolecules. Mill Valley, Calif: University Science Books, 1990.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
10

Krishna, Mallia A., and Smith Paul K, eds. Immobilized affinity ligand techniques. San Diego: Academic Press, 1992.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Book chapters on the topic "Binding sites (Biochemistry) Ligand binding (Biochemistry)"

1

Heidrich, Corina G., and Christian Berens. "Probing RNA Structure and Ligand Binding Sites on RNA by Fenton Cleavage." In Handbook of RNA Biochemistry, 301–18. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2014. http://dx.doi.org/10.1002/9783527647064.ch15.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Chance, B., L. Powers, M. Chance, Y. Zhou, and K. S. Reddy. "Optical and X-Ray Techniques in the Study of Rapid Ligand Binding: A Ligand „Docking“ Site in the Reaction of Mb and Co At 40 K." In Advances in Membrane Biochemistry and Bioenergetics, 419–28. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4684-8640-7_40.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Lasseter, Benjamin F. "Fluorescence Studies of Ligand Binding." In Biochemistry in the Lab, 159–68. Names: Lasseter, Benjamin F., author. Title: Biochemistry in the lab : a manual for undergraduates / by Benjamin F. Lasseter. Description: Boca Raton, Florida : CRC Press, [2020]: CRC Press, 2019. http://dx.doi.org/10.1201/9780429491269-16.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Vinson, Charles, Raghunath Chatterjee, and Peter Fitzgerald. "Transcription Factor Binding Sites and Other Features in Human and Drosophila Proximal Promoters." In Subcellular Biochemistry, 205–22. Dordrecht: Springer Netherlands, 2011. http://dx.doi.org/10.1007/978-90-481-9069-0_10.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Åqvist, Johan, Osvaldo Alvarez, and George Eisenman. "Computer Modelling of Ion Binding Sites in Proteins." In The Jerusalem Symposia on Quantum Chemistry and Biochemistry, 367–82. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2718-9_29.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Betz, H., V. Schmieden, and J. Kuhse. "Determinants of Ligand Binding to the Inhibitory Glycine Receptor." In The Jerusalem Symposia on Quantum Chemistry and Biochemistry, 241–47. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2718-9_21.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Harris, Dinari A., Gabrielle C. Todd, and Nils G. Walter. "Terbium(III) Footprinting as a Probe of RNA Structure and Metal Binding Sites." In Handbook of RNA Biochemistry, 255–68. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2014. http://dx.doi.org/10.1002/9783527647064.ch12.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Nelson, David L. "Biochemistry and Pharmacology of the 5-HT1 Serotonin Binding Sites." In The Serotonin Receptors, 23–57. Totowa, NJ: Humana Press, 1988. http://dx.doi.org/10.1007/978-1-4612-4560-5_2.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Hoell, Jessica I., Markus Hafner, Markus Landthaler, Manuel Ascano, Thalia A. Farazi, Greg Wardle, Jeff Nusbaum, et al. "Transcriptome-Wide Identification of Protein Binding Sites on RNA by PAR-CLIP (Photoactivatable-Ribonucleoside-Enhanced Crosslinking and Immunoprecipitation)." In Handbook of RNA Biochemistry, 877–98. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2014. http://dx.doi.org/10.1002/9783527647064.ch39.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "Binding sites (Biochemistry) Ligand binding (Biochemistry)"

1

Villanueva, German B., Konno Sensuke, and John Fenton. "EVIDENCE FOR MULTIPLE BINDING SITES OF HIRUDIN IN THROMBIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644666.

Full text
Abstract:
A highly purified hirudin with a specific activity of 13, 950 AT units/mg was used in these studies. Investigation of the circular dichroism of hirudin and thrombin showed that the CD spectrum of the thrombin-hirudin complex deviates significantly from additivity towards a less organized structure (i.e. loss of a-helix).A sigmoidal curve, rather than a hyperbolic curve, is generated when the deviation from additivity is plotted against hirudin concentration. This suggests cooperativity of the binding process. At low concentation, aScatchard plot of the data fits intoa straight line clearly indicating one binding site per mole of thrombin.This site binds hirudin with a dissociation constant of 500 nM. However, the data cannot be fitted to a straight line at higher concentration ofhirudin suggesting that hirudin binds also to another site with a different affinity. These results agree with the findings of Stone and Hofsteenge (Biochemistry 25, 4622-4628, 1986) and support the idea that initially hirudin binds at a site distinct from the active site, which then rearranges through a conformational change (detected by CD) to form a tigher complex in which hirudin is also bound to the active site.
APA, Harvard, Vancouver, ISO, and other styles
2

Kuyas, C., H. Sigrist, and P. W. Straub. "LOCALIZATION CF FIBRIN POLYMERIZATION SITES BY PHOTQAFFINITY LABELING." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643776.

Full text
Abstract:
Fibrin polymerization is competitively inhibited by the te-trapeptide GlyProArgPro. This peptide corresponds to the N-terminal sequence of the fibrin α-polypeptide chain, which is exposed upon release of fibrinopeptide A by thrombin. A binding site for GlyProArgPro was suggested to be located in the C-terminal end of the 411 amino acids containing γ-chain (Varadi and Scheraga, Biochemistry, 25, 519, 1986). In order to characterize the polymerization domain, GlyProArgProLys-azidoazobenzene, a photoactivable derivative of GlyProArgPro was synthesized. Photoaffinity label was bound to fibrinogen in the dark and photolysis was carried out at 0°C. After reduction and S-carboxymethy-lation of the photoaffinity labeled fibrinogen, the polypeptide chains (Aα, Bβ,γ ) were separated by ion-exchange chromatography. Photolabel binding was monitored imnunologically with anti-azo-benzene antibodies (ELISA, Western blot). Selective labeling of the γ-chain was observed. Labeled γ-chains were further digested with CNBr, and the resulting fragments were separated by reversed phase HPIC, immunologically characterized and identified by Edman degradation. GlyProArgProLys-azidoazobenzene was incorporated in the 18 kD CNBr-fragment (γ95-264). The CNBr-fragments arising from C-terminal end of the γ-chain were not labeled.Our results indicate that the binding site of GlyProArgPro is localized exclusively on γ-chain, within the sequence γ95-264.
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Binding sites (Biochemistry) Ligand binding (Biochemistry)' for particular source types:
Journal articles Dissertations / Theses Books
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography