(Q73009412)

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The thermodynamics of protein-protein recognition as characterized by a combination of volumetric and calorimetric techniques: the binding of turkey ovomucoid third domain to alpha-chymotrypsin

scientific article published on 01 February 2003

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31 October 2019

The thermodynamics of protein-protein recognition as characterized by a combination of volumetric and calorimetric techniques: the binding of turkey ovomucoid third domain to alpha-chymotrypsin (English)

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31 October 2019

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Rana Filfil

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31 October 2019

Tigran V Chalikian

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31 October 2019

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1 February 2003

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31 October 2019

Journal of Molecular Biology

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31 October 2019

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31 October 2019

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31 October 2019

1271-1288

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31 October 2019

Protein inhibitors of proteinases

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The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3)

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Solution structure of turkey ovomucoid third domain as determined from nuclear magnetic resonance data

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Structure of the complex of Streptomyces griseus protease B and the third domain of the turkey ovomucoid inhibitor at 1.8-A resolution

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7 January 2021

Crystal and molecular structures of the complex of alpha-chymotrypsin with its inhibitor turkey ovomucoid third domain at 1.8 A resolution

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7 January 2021

Dissecting the energetics of a protein-protein interaction: the binding of ovomucoid third domain to elastase

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Calorimetric investigations of the binding of inhibitors to alpha-chymotrypsin. I. The enthalpy of dilution of alpha-chymotrypsin and of proflavin, and the enthalpy of binding of indole, N-acetyl-D-tryptophan, and proflavin to alpha-chymotrypsin

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7 January 2021

Structure of alpha-chymotrypsin refined at 1.68 A resolution

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7 January 2021

Effect of sucrose on the dimerization of alpha-chymotrypsin. Allowance for thermodynamic nonideality arising from the presence of a small inert solute.

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7 January 2021

Effects of molecular crowding by saccharides on alpha-chymotrypsin dimerization

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Compressibility-structure relationship of globular proteins.

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Hydration and partial compressibility of biological compounds

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The hydration of globular proteins as derived from volume and compressibility measurements: cross correlating thermodynamic and structural data

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Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry

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Thermodynamics of the interaction of barnase and barstar: changes in free energy versus changes in enthalpy on mutation

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Isothermal titration calorimetry of protein-protein interactions

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Coupling of local folding to site-specific binding of proteins to DNA

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Structure-based prediction of binding affinities and molecular design of peptide ligands.

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Heat capacity and compactness of denatured proteins

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Heat capacity of hydrogen-bonded networks: an alternative view of protein folding thermodynamics.

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7 January 2021

Thermodynamics and kinetics of single residue replacements in avian ovomucoid third domains: effect on inhibitor interactions with serine proteinases

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7 January 2021

On volume changes accompanying conformational transitions of biopolymers

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7 January 2021

Volumetric properties of proteins

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Thermodynamic analysis of biomolecules: a volumetric approach

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Areas, volumes, packing and protein structure

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Calculation of molecular volumes and areas for structures of known geometry.

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Analytical molecular surface calculation

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Solvent-accessible surfaces of proteins and nucleic acids

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Compressibility of protein transitions

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Empirical scale of side-chain conformational entropy in protein folding

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The backbone conformational entropy of protein folding: experimental measures from atomic force microscopy.

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Protein-DNA recognition: new perspectives and underlying themes

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Hydration in drug design. 1. Multiple hydrogen-bonding features of water molecules in mediating protein-ligand interactions

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Sequence-specific DNA-binding dominated by dehydration

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The role of water in protein-DNA interactions

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Linkage of EcoRI dissociation from its specific DNA recognition site to water activity, salt concentration, and pH: separating their roles in specific and non-specific binding.

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Thermodynamics of unfolding for turkey ovomucoid third domain: thermal and chemical denaturation

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The Protein Data Bank

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Volume changes on protein folding.

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Identifiers

10.1016/S0022-2836(03)00022-6

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12589768%20AND%20SRC:MED&resulttype=core&format=json

31 October 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12589768%20AND%20SRC:MED&resulttype=core&format=json

31 October 2019

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