Nonnative interactions in the FF domain folding pathway from an atomic resolution structure of a sparsely populated intermediate: An NMR relaxation dispersion study

Journal of the American Chemical Society

Volumn 133, Issue 28, 2011, Pages 10974-10982

  Korzhnev, Dmitry M ^a,b   Vernon, Robert M ^c   Religa, Tomasz L ^a   Hansen, Alexandar L ^a   Baker, David ^c   Fersht, Alan R ^d   Kay, Lewis E ^a  

^a UNIVERSITY OF TORONTO   (Canada)

^b UNIVERSITY OF CONNECTICUT HEALTH CENTER   (United States)

^c UNIVERSITY OF WASHINGTON   (United States)

^d MEDICAL RESEARCH COUNCIL   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE BOND; ATOMIC RESOLUTION; ATOMIC RESOLUTION STRUCTURES; EXPERIMENTAL STUDIES; FOLDING INTERMEDIATES; FOLDING PATHWAY; FOLDING TRANSITION STATE; INTERMEDIATE STATE; INTERMEDIATE STRUCTURES; NATIVE CONFORMATION; NATIVE STATE; NMR RELAXATION DISPERSION; NON-NATIVE INTERACTIONS; RELAXATION DISPERSION; ROOM TEMPERATURE; SINGLE-DOMAIN PROTEINS; TIME-SCALES; WILD TYPES;

AMIDES; CONFORMATIONS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

DISPERSIONS;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHEMICAL BOND; CHEMICAL INTERACTION; CHEMICAL REACTION; DISPERSION; HETERONUCLEAR MULTIPLE QUANTUM COHERENCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTON TRANSPORT; ROOM TEMPERATURE; STRUCTURE ANALYSIS; THERMODYNAMICS; WILD TYPE;

CARRIER PROTEINS; KINETICS; MODELS, MOLECULAR; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; THERMODYNAMICS;

EID: 79960208648     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja203686t     Document Type: Article

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