Charge-charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa

Protein Science

Volumn 14, Issue 7, 2005, Pages 1934-1938

  Trefethen, Jared M ^a   Pace, C Nick ^a,b   Scholtz, J Martin ^a,b   Brems, David N ^c  

^a TEXAS A AND M UNIVERSITY   (United States)

^b TEXAS A M COLLEGE OF MEDICINE   (United States)

^c AMGEN INC   (United States)

Author keywords

Charge charge interactions; Denatured state; Folding kinetics; Protein folding; Protein stability

Indexed keywords

RIBONUCLEASE;

ANALYTIC METHOD; ARTICLE; DENATURATION; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE;

ENZYME STABILITY; ISOENZYMES; KINETICS; MUTATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; RIBONUCLEASES;

EID: 22244458003     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.051401905     Document Type: Article

References (21)

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