Examination of the folding of E. coli CspA through tryptophan substitutions

Protein Science

Volumn 10, Issue 10, 2001, Pages 2028-2036

  Vu, Dung M ^a   Reid, Katherine L ^a,b   Rodriguez, Hector M ^a   Gregoret, Lydia M ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b PROTEIN DESIGN LABS INC   (United States)

Author keywords

Aromatic cluster; Cold shock protein; Folding kinetics; Sheet assembly; Stopped flow fluorescence; Two state folding

Indexed keywords

BACTERIAL PROTEIN; COLD SHOCK PROTEIN; COLD SHOCK PROTEIN A; NUCLEIC ACID; TRYPTOPHAN; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CLUSTER ANALYSIS; ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; INFRARED SPECTROSCOPY; KINETICS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; TEMPERATURE DEPENDENCE;

AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; ESCHERICHIA COLI; KINETICS; MODELS, MOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, FLUORESCENCE; TEMPERATURE; TRYPTOPHAN;

EID: 0034802586     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.16201     Document Type: Article

References (28)

1. Correction for light absorption in fluorescence studies of protein-ligand interactions
2. The backbone structure of the major cold-shock protein CS7.4 of Escherichia coli in solution includes extensive β-sheet structure
3. Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations
4. Folding kinetics of T4 lysozyme and nine mutants at 12 degrees C
5. Cavity formation before stable hydrogen bonding in the folding of a β-Clam protein
6. Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) from Escherichia coli: Evidence for conformational dynamics in the single-stranded RNA-binding site
7. Coupling of protein stability and protein function in E. coli CspA
8. How do small single-domain proteins fold?
9. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
10. MOLSCRIPT - A program to produce both detailed and schematic plots of protein structures
11. Mutant sequences as probes of protein folding mechanisms
12. Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: Identification of a binding epitope for DNA
13. Mechanism of protein folding
14. Determination and analysis of urea and guanidine hydrochloride denaturation curves
15. How to measure and predict the molar absorption coefficient of a protein
16. Conservation of rapid two-state folding in mesophilic, thermophilic, and hyperthermophilic cold shock proteins
17. Topology, stability, sequence, and length: Defining the determinants of two-state protein folding kinetics
18. Stability and folding properties of a model β-sheet protein, Escherichia coli CspA
19. Role of a solvent-exposed aromatic cluster in the folding of Escherichia coli CspA
20. DNA sequencing with chain-terminating inhibitors
21. Solvent denaturation
22. Crystal structure of CspA, the major cold shock protein of Escherichia coli
23. Thermodynamic properties of an extremely rapid protein folding reaction
24. Extremely rapid protein folding in the absence of intermediates
25. Protein denaturation
26. Protein denaturation. C. Theoretical models for the mechanism of denaturation
27. Protein folding and unfolding on a complex energy landscape
28. Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition