Deletion of a single amino acid changes the folding of an apamin hybrid sequence peptide to that of endothelin

Biopolymers

Volumn 41, Issue 4, 1997, Pages 451-460

  Volkman, Brian F ^a   Wemmer, David E ^a  

^a LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL BONDS; CONFORMATIONS; CROSSLINKING; CRYSTAL ATOMIC STRUCTURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEIC ACID SEQUENCES; POLYPEPTIDES; SULFUR COMPOUNDS;

APAMIN DELETION (AD) PEPTIDES; APAMIN HYBRID SEQUENCE PEPTIDES; CYSTEINES; ENDOTHELIN;

AMINO ACIDS;

ENDOTHELIN; NEUROTOXIN;

AMINO ACID ANALYSIS; AMINO ACID SEQUENCE; ARTICLE; DISULFIDE BOND; NUCLEAR MAGNETIC RESONANCE; PEPTIDE SYNTHESIS; PROTEIN ANALYSIS; PROTEIN CROSS LINKING; PROTEIN FOLDING; PROTEIN PURIFICATION; SEQUENTIAL ANALYSIS; STATISTICAL ANALYSIS;

ANIMALS; APAMIN; ENDOTHELIN-1; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; SEQUENCE DELETION;

APOIDEA;

EID: 0031553985     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1097-0282(19970405)41:4<451::aid-bip9>3.0.co;2-l     Document Type: Article

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