Compressibility gives new insight into protein dynamics and enzyme function

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1595, Issue 1-2, 2002, Pages 382-386

  Gekko, Kunihiko ^a  

^a HIROSHIMA UNIVERSITY   (Japan)

Author keywords

Adiabatic compressibility; Amino acid substitution; Cavity; Enzyme function; Ligand binding; Protein dynamics

Indexed keywords

DIHYDROFOLATE REDUCTASE; DIHYDROFOLIC ACID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

AMINO ACID SUBSTITUTION; COENZYME; COMPRESSION; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; LIGAND BINDING; MOLECULAR DYNAMICS; MUTATION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; REVIEW; X RAY CRYSTALLOGRAPHY;

AMINO ACID SUBSTITUTION; ENZYMES; LIGANDS; PRESSURE; PROTEINS;

EID: 0037171121     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(01)00358-2     Document Type: Review

References (17)

1. Thermodynamic fluctuations in protein molecules
2. Compressibility of globular proteins in water at 25°C
3. Compressibility-structure relationship of globular proteins
4. Volumetric characterizations of the native, molten globule and unfolded states of cytochrome c at acidic pH
5. Partial volumes and compressibilities of extended polypeptide chains in aqueous solution: Additivity scheme and implication of protein unfolding at normal and high pressure
6. Compressibility and volume changes of lysozyme due to inhibitor binding
7. Effect of ligand binding on the flexibility of dihydrofolate reductase as revealed compressibility
8. A large compressibility change of protein induced by a single amino acid substitution
9. Single amino acid substitutions in flexible loops can induce large compressibility changes in dihydrofolate reductase
10. Fluctuation of the lysozyme structure: (II) Effects of temperature and binding of inhibitors
11. Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli
12. Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
13. High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase
14. Point mutations at glycine-121 of Escherichia coli dihydrofolate reductase: Important roles of a flexible loop in the stability and function
15. Effects of point mutations at the flexible loop of Escherichia coli dihydrofolate reductase on its stability and function
16. Effects of point mutations at the flexible loop alanine-145 of Escherichia coli dihydrofolate reductase on its stability and function
17. Nonadditive effects of double mutations at the flexible loops, glycine-67 and glycine-121, of Escherichia coli dihydrofolate reductase on its stability and function