Comparison of the folding processes of T. thermophilus and E. coli Ribonucleases H

Journal of Molecular Biology

Volumn 316, Issue 2, 2002, Pages 327-340

  Hollien, Julie ^a   Marqusee, Susan ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Hydrogen exchange; Protein folding; Protein stability; Ribonuclease H; Thermophilic

Indexed keywords

PROLINE; PROTEIN; PROTON; RIBONUCLEASE H;

ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME STABILITY; ESCHERICHIA COLI; FLUORESCENCE; ION EXCHANGE; ISOMERISM; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; SPECIES COMPARISON; THERMUS THERMOPHILUS;

ESCHERICHIA COLI; THERMUS; THERMUS THERMOPHILUS;

EID: 0036295079     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.5346     Document Type: Article

References (37)

1. Topology, stability, sequence, and length: Defining the determinants of two-state protein folding kinetics
2. Contact order, transition state placement and the refolding rates of single domain proteins
3. Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding
4. The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved
5. Experiment and theory highlight role of native state topology in SH3 folding
6. Folding of beta-sandwich proteins: Three-state transition of a fibronectin type III module
7. Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9
8. Conservation of folding pathways in evolutionarily distant globin sequences
9. The refolding of human lysozyme: A comparison with the structurally homologous hen lysozyme
10. Comparison of equilibrium and kinetic approaches for determining protein folding mechanisms
11. The energetics of T4 lysozyme reveal a hierarchy of conformations
12. Detection and characterization of an early folding intermediate of T4 lysozyme using pulsed hydrogen exchange and two-dimensional NMR
13. Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins
14. The unusually slow unfolding rate causes the high stability of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus: Equilibrium and kinetic studies of guanidine hydrochloride-induced unfolding and refolding
15. Stability and folding of dihydrofolate reductase from the hyperthermophilic bacterium Thermotoga maritima
16. Kinetic role of electrostatic interactions in the unfolding of hyperthermophilic and mesophilic rubredoxins
17. The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions
18. Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH
19. Crystal structure of ribonuclease H from Thermus thermophilus HB8 refined at 2.8 Å resolution
20. Structural distribution of stability in a thermophilic enzyme
21. Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: A comparative study of the folding reactions of alpha-lactalbumin and lysozyme
22. Unfolding free energy changes determined by the linear extrapolation method: 1. Unfolding of phenylmethanesulfonyl-alpha-chymotrypsin using different denaturants
23. Cis-trans isomerization of proline residues
24. Fast-folding and slow-folding forms of unfolded proteins
25. Test of the extended two-state model for the kinetic intermediates observed in the folding transition of ribonuclease A
26. On-pathway versus off-pathway folding intermediates
27. Protein conformational stabilities can be determined from hydrogen exchange rates
28. NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A
29. Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR
30. Structure and stability of cytochrome c folding intermediates
31. Primary structure effects on peptide group hydrogen exchange
32. The sequences of small proteins are not extensively optimized for rapid folding by natural selection
33. Effect of prolyl isomerase on the folding reactions of staphylococcal nuclease
34. Folding of chymotrypsin inhibitor 2.2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding
35. Cis/trans isomerization at proline: Desolvation and its consequences for protein folding
36. A thermodynamic comparison of mesophilic and thermophilic ribonucleases H
37. Rapid and efficient site-specific mutagenesis without phenotypic selection