Hairpin folding dynamics: The cold-denatured state is predisposed for rapid refolding

Biochemistry

Volumn 44, Issue 30, 2005, Pages 10406-10415

  Dyer, R Brian ^a   Maness, Shelia J ^b   Franzen, Stefan ^b   Fesinmeyer, R Matthew ^c   Olsen, Katherine A ^c   Andersen, Niels H ^c  

^a LOS ALAMOS NATIONAL LABORATORY   (United States)

^b NORTH CAROLINA STATE UNIVERSITY   (United States)

^c UNIVERSITY OF WASHINGTON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACCELERATION; AMINO ACIDS; BIOCHEMISTRY; CHARACTERIZATION; INFRARED SPECTROSCOPY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SOLVENTS;

COLD DENATURATION; GLOBULAR PROTEINS; HAIRPIN FORMING PEPTIDES; HEAT DENATURED STATE;

PROTEINS;

GLOBULAR PROTEIN; HEXAFLUORO 2 PROPANOL;

ARTICLE; CIRCULAR DICHROISM; COLD DENATURATION; INFRARED SPECTROSCOPY; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE; TEMPERATURE DEPENDENCE;

CIRCULAR DICHROISM; COLD; HEAT; HUMANS; HYDROGEN BONDING; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, CHEMICAL; PEPTIDES; PROPANOLS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; THERMODYNAMICS;

EID: 23044464791     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050698z     Document Type: Article

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