Role of a nonnative interaction in the folding of the protein G B1 domain as inferred from the conformational analysis of the α-helix fragment

Folding and Design

Volumn 2, Issue 2, 1997, Pages 123-133

  Blanco, Francisco J ^a   Ortiz, Angel R ^a,b   Serrano, Luis ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Hydrophobia staple motif; Peptide conformation; Protein G; Schellman motif; helix

Indexed keywords

BACTERIAL PROTEIN; IGG FC BINDING PROTEIN, STREPTOCOCCUS; IGG FC-BINDING PROTEIN, STREPTOCOCCUS; PEPTIDE FRAGMENT; TRIFLUOROETHANOL;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; COMPUTER SIMULATION; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SOLUTION AND SOLUBILITY;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CIRCULAR DICHROISM; COMPUTER SIMULATION; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SOLUTIONS; TRIFLUOROETHANOL;

EID: 0030623419     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(97)00017-5     Document Type: Article

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