Refolding kinetics of cytochrome c551 reveals a mechanistic difference between urea and guanidine

Protein Science

Volumn 10, Issue 8, 2001, Pages 1685-1688

  Gianni, Stefano ^a   Brunori, Maurizio ^a   Travaglini Allocatelli, Carlo ^a  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

Author keywords

Denaturants; Guanidinium binding; Kinetics; Mutants; Protein folding; Stability

Indexed keywords

CYTOCHROME C; GUANIDINE; UREA;

ARTICLE; NONLINEAR SYSTEM; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PSEUDOMONAS AERUGINOSA; SITE DIRECTED MUTAGENESIS;

BACTERIAL PROTEINS; CYTOCHROME C GROUP; GUANIDINE; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN DENATURATION; PROTEIN FOLDING; PSEUDOMONAS AERUGINOSA; UREA;

EID: 0034917762     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.5101     Document Type: Article

References (12)

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2. 551 from Pseudomonas aeruginosa
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4. Protein stability as a function of denaturant concentration: Thermal stability of barnase in the presence of urea
5. Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A
6. Comparison of antiparallel and parallel two-stranded α-helical chains in two stranded α-helical coiled-coils: Design, synthesis, and characterization
7. Protein denaturation with guanidine hydrocloride or urea provides a different estimate of stability depending on the contribution of electrostatic interactions
8. Measuring and increasing protein stability
9. Effects of denaturants at low concentrations on the reversible denaturation of staphylococcal nuclease
10. 551: Role of electrostatic interactions on the hydrophobic collapse and transition state properties
11. New evidence for the denaturant binding model