NMR characterization of a peptide model provides evidence for significant structure in the unfolded state of the villin headpiece helical subdomain

Biochemistry

Volumn 45, Issue 22, 2006, Pages 6940-6946

  Tang, Yuefeng ^a   Goger, Michael J ^b   Raleigh, Daniel P ^a  

^a STONY BROOK UNIVERSITY   (United States)

^b NEW YORK STRUCTURAL BIOLOGY CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; HYDROGEN BONDS; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS; PROTONS;

COUPLING CONSTANTS; HEADPIECE SUBDOMAIN; HELICAL SUBDOMAIN; UNFOLDED STATES;

POLYPEPTIDES;

CELL PROTEIN; PROTEIN HP21; PROTEIN HP36; UNCLASSIFIED DRUG; VILLIN; VILLIN HEADPIECE SUBDOMAIN PROTEIN;

ALPHA HELIX; ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR INTERACTION; MOLECULAR MODEL; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; TEMPERATURE DEPENDENCE;

AMINO ACID SEQUENCE; DROSOPHILA PROTEINS; MAGNETIC RESONANCE SPECTROSCOPY; MICROFILAMENT PROTEINS; MOLECULAR SEQUENCE DATA; NEUROFILAMENT PROTEINS; PEPTIDE FRAGMENTS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 33744960040     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi052484n     Document Type: Article

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