NMR and SAXS characterization of the denatured state of the chemotactic protein CheY: Implications for protein folding initiation

Protein Science

Volumn 10, Issue 6, 2001, Pages 1100-1112

  Garcia, Pascal ^a   Serrano, Luis ^b   Durand, Dominique ^c   Rico, Manuel ^a   Bruix, Marta ^a  

^a INSTITUTO DE ESTRUCTURA DE LA MATERIA   (Spain)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^c UNIVERSITÉ PARIS SACLAY   (France)

Author keywords

Backbone dynamics; Denatured state; Folding initiation; Heteronuclear NMR; Residual structures

Indexed keywords

CHEMOTACTIC PEPTIDE; CHEMOTACTIC PROTEIN CHEY; PROTEIN; PROTEIN SUBUNIT; UNCLASSIFIED DRUG; UREA;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; GENETIC ENGINEERING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; X RAY CRYSTALLOGRAPHY;

BACTERIAL PROTEINS; ESCHERICHIA COLI; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANE PROTEINS; MODELS, MOLECULAR; MODELS, THEORETICAL; MUTATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SCATTERING, RADIATION; UREA; X-RAYS;

EID: 0035017534     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.52701     Document Type: Article

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