Experimental assignment of the structure of the transition state for the association of barnase and barstar

Journal of Molecular Biology

Volumn 308, Issue 1, 2001, Pages 69-77

  Frisch, Christian ^a   Fersht, Alan R ^a   Schreiber, Gideon ^b  

^a MEDICAL RESEARCH COUNCIL   (United Kingdom)

^b WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

Association; Double mutant cycles; Protein engineering; Protein protein interaction

Indexed keywords

BARNASE; BARSTAR;

ARTICLE; BINDING SITE; DIFFUSION; ENTHALPY; ENTROPY; ENZYME ANALYSIS; ENZYME STRUCTURE; GENETIC ENGINEERING; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN PROTEIN INTERACTION; REACTION ANALYSIS; SOLVATION; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE; THERMODYNAMICS;

BACTERIA (MICROORGANISMS);

EID: 0035917323     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.4577     Document Type: Article

References (28)

1. Protein-protein recognition: Crystal structural analysis of a barnase-barstar complex at 2.0-Å resolution
2. Free energy landscapes of encounter complexes in protein-protein association
3. Kinetics of desolvation-mediated protein-protein binding
4. The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus)
5. Thermodynamics of the interaction of barnase and barstar: Changes in free energy versus changes in enthalpy on mutation
6. Simulation of the diffusional association of barnase and barstar
7. On the protein-protein diffusional encounter complex
8. Non-additivity in protein-protein interactions
9. Co-operative interactions during protein folding
10. Strength and cooperativity of contributions of surface salt bridges to protein stability
11. Mutations in the complementarity-determining regions do not cause differences in free energy during the process of formation of the activated complex between an antibody and the corresponding protein antigen
12. The kinetics of protein-protein recognition
13. Kinetics of protein-nucleic acid interactions: Use of salt effects to probe mechanisms of interaction
14. Negative activation enthalpies in the kinetics of protein folding
15. Stabilization of protein structure by interaction of an alpha-helix dipole with a charged side-chain
16. The interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering
17. Energetics of protein-protein interactions: Analysis of the barnasebarstar interface by single mutations and double mutant cycles
18. Rapid, electrostatic assisted, association of proteins
19. Stability versus function: Two competing forces in the evolution of barstar
20. Predicting the rate enhancement of protein complex formation from the electrostatic energy of interaction
21. Rational design of faster associating and tighter binding protein complexes
22. Estimating the contribution of engineered surface electrostatic interactions to protein stability using double-mutant cycles
23. Electrostatic enhancement of diffusion-controlled protein-protein association: Comparison of theory and experiment on barnase and barstar
24. Association and dissociation kinetics of anti-hen egg lysozyme monoclonal antibodies HyHEL-5 and HyHEL-10