Related ArticlesDissecting functional interactions in coagulation protein complexes by use of NMR spectroscopy.
Curr Protein Pept Sci. 2002 Jun;3(3):275-85
Authors: Tolkatchev D, Koutychenko A, Ni F
The blood coagulation cascade can be considered as a system of well-orchestrated protein activation reactions involving and leading to the formation of large macromolecular assemblies. NMR investigations performed during the last six years have focused on the structural, motional and binding properties of some protein domains and interfaces critical for the formation of these protein complexes, outlining sophisticated intermolecular adaptations. The studied protein domains are either single molecules or covalently-linked heterodimers of the epidermal growth factor (EGF) homology domains, calcium-binding EGF domains and gamma-carboxyglutamic(Gla)-containing domains responsible for calcium-dependent binding to cell membranes. The characterized binding interfaces have included those between thrombin and fibrinogen, between thrombin and thrombomodulin, between factor VIIIa and the cell membrane, between tissue factor and factor VIIa, and most recently between factor Va and prothrombin. The obtained results indicate that the regulation of blood coagulation by protein and low molecular weight cofactors may involve a significant degree of protein folding transitions with changes in molecular and conformational motions coupled to enzymatic activities. This new level of complexity of the molecular processes controlling coagulation may lead to novel strategies for the development of more effective therapeutic anticoagulants.
Dissecting electrostatic interactions in Bacillus circulans xylanase through NMR-monitored pH titrations
Dissecting electrostatic interactions in Bacillus circulans xylanase through NMR-monitored pH titrations
Abstract NMR-monitored pH titration curves of proteins provide a rich source of structural and electrostatic information. Although relatively straightforward to measure, interpreting pH-dependent chemical shift changes to obtain site-specific acid dissociation constants (pK A values) is challenging. In order to analyze the biphasic titrations exhibited by the side chain 13Cγ nuclei of the nucleophilic Glu78 and general acid/base Glu172 in Bacillus circulans xylanase, we have...
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Dissecting electrostatic interactions in Bacillus circulans xylanase through NMR-monitored pH titrations.
Dissecting electrostatic interactions in Bacillus circulans xylanase through NMR-monitored pH titrations.
Dissecting electrostatic interactions in Bacillus circulans xylanase through NMR-monitored pH titrations.
J Biomol NMR. 2011 Sep;51(1-2):5-19
Authors: McIntosh LP, Naito D, Baturin SJ, Okon M, Joshi MD, Nielsen JE
Abstract
NMR-monitored pH titration curves of proteins provide a rich source of structural and electrostatic information. Although relatively straightforward to measure, interpreting pH-dependent chemical shift changes to...
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09-30-2011 06:00 AM
Dissecting electrostatic interactions in Bacillus circulans xylanase through NMR-monitored pH titrations.
Dissecting electrostatic interactions in Bacillus circulans xylanase through NMR-monitored pH titrations.
Dissecting electrostatic interactions in Bacillus circulans xylanase through NMR-monitored pH titrations.
J Biomol NMR. 2011 Sep;51(1-2):5-19
Authors: McIntosh LP, Naito D, Baturin SJ, Okon M, Joshi MD, Nielsen JE
Abstract
NMR-monitored pH titration curves of proteins provide a rich source of structural and electrostatic information. Although relatively straightforward to measure, interpreting pH-dependent chemical shift changes...
[NMR paper] Dissecting structural and electrostatic interactions of charged groups in alpha-sarci
Dissecting structural and electrostatic interactions of charged groups in alpha-sarcin. An NMR study of some mutants involving the catalytic residues.
Related Articles Dissecting structural and electrostatic interactions of charged groups in alpha-sarcin. An NMR study of some mutants involving the catalytic residues.
Biochemistry. 2003 Nov 18;42(45):13122-33
Authors: García-Mayoral MF, Pérez-Cañadillas JM, Santoro J, Ibarra-Molero B, Sanchez-Ruiz JM, Lacadena J, Martínez del Pozo A, Gavilanes JG, Rico M, Bruix M
The cytotoxic ribonuclease...
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[NMR paper] Probing site-specific interactions in protein-DNA complexes using heteronuclear NMR s
Probing site-specific interactions in protein-DNA complexes using heteronuclear NMR spectroscopy and molecular modeling: binding of Cro repressor to OR3.
Related Articles Probing site-specific interactions in protein-DNA complexes using heteronuclear NMR spectroscopy and molecular modeling: binding of Cro repressor to OR3.
J Biomol Struct Dyn. 1998 Aug;16(1):13-20
Authors: Edwards CA, Tung CS, Silks LA, Gatewood JM, Fee JA, Mariappan SV
In this paper, a general method is developed to study site-specific interactions in DNA-protein complexes...
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[NMR paper] NMR for the design of functional mimetics of protein-protein interactions: one key is
NMR for the design of functional mimetics of protein-protein interactions: one key is in the building of bridges.
Related Articles NMR for the design of functional mimetics of protein-protein interactions: one key is in the building of bridges.
Biochem Cell Biol. 1998;76(2-3):177-88
Authors: Song J, Ni F
Using the design of bivalent and bridge-binding inhibitors of thrombin as an example, we review an NMR-based experimental approach for the design of functional mimetics of protein-protein interactions. The strategy includes: (i) identification...
Dissecting functional interactions in coagulation protein complexes by use of NMR spe
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