NMR and temperature-jump measurements of de novo designed proteins demonstrate rapid folding in the absence of explicit selection for kinetics.

Journal of molecular biology

Volumn 330, Issue 4, 2003, Pages 813-819

  Gillespie, Blake ^a   Vu, Dung M ^a   Shah, Premal S ^a   Marshall, Shannon A ^a   Dyer, R Brian ^a   Mayo, Stephen L ^a   Plaxco, Kevin W ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

UREA;

ALGORITHM; AMINO ACID SEQUENCE; ARTICLE; COMPUTER PROGRAM; DOSE RESPONSE; ESCHERICHIA COLI; KINETICS; METABOLISM; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; TEMPERATURE; THERMODYNAMICS; TIME;

ALGORITHMS; AMINO ACID SEQUENCE; DOSE-RESPONSE RELATIONSHIP, DRUG; ESCHERICHIA COLI; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; SOFTWARE; TEMPERATURE; THERMODYNAMICS; TIME FACTORS; UREA;

EID: 0041530316     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00616-8     Document Type: Article

References (0)