Conformational analysis of peptide fragments derived from the peripheral subunit-binding domain from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus: Evidence for nonrandom structure in the unfolded state

Biopolymers

Volumn 49, Issue 1, 1999, Pages 29-40

  Spector, Shari ^a   Rosconi, Michael ^a   Raleigh, Daniel P ^a  

^a STONY BROOK UNIVERSITY   (United States)

Author keywords

Bacillus stearothermophilus; Peptide fragments; Peripheral subunit binding domain; Protein folding; Pyruvate dehydrogenase multienzyme complex; Unfolded state

Indexed keywords

CONFORMATIONS; HYDROGEN BONDS; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

CHEMICAL SHIFTS; PEPTIDE; PROTEIN FOLDING;

ENZYMES;

PYRUVATE DEHYDROGENASE;

ARTICLE; COMPLEX FORMATION; ENZYME CONFORMATION; GEOBACILLUS STEAROTHERMOPHILUS; MOLECULAR INTERACTION; NONHUMAN; PROTEIN FOLDING;

AMINO ACID SEQUENCE; BACILLUS STEAROTHERMOPHILUS; BACTERIAL PROTEINS; BINDING SITES; CIRCULAR DICHROISM; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PYRUVATE DEHYDROGENASE COMPLEX; SEQUENCE HOMOLOGY, AMINO ACID;

GEOBACILLUS STEAROTHERMOPHILUS;

EID: 0032905913     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0282(199901)49:1<29::AID-BIP4>3.0.CO;2-7     Document Type: Article

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