Conformational investigation of designed short linear peptides able to fold into β-hairpin structures in aqueous solution

Folding and Design

Volumn 1, Issue 2, 1996, Pages 133-144

  De Alba, Eva ^a   Jiménez, M Angeles ^a   Rico, Manuel ^a   Nieto, José L ^a  

^a INSTITUTO DE ESTRUCTURA DE LA MATERIA   (Spain)

Author keywords

NMR; Peptide design; Peptide structure; hairpin conformation

Indexed keywords

OLIGOPEPTIDE; TRIFLUOROETHANOL; WATER;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG DESIGN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SOLUTION AND SOLUBILITY; SYNTHESIS;

AMINO ACID SEQUENCE; DRUG DESIGN; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR STRUCTURE; OLIGOPEPTIDES; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SOLUTIONS; TRIFLUOROETHANOL; WATER;

EID: 0030334822     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/s1359-0278(96)00022-3     Document Type: Article

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