Position effect of cross-strand side-chain interactions on β-hairpin formation

Protein Science

Volumn 9, Issue 11, 2000, Pages 2151-2160

  Santiveri, C M ^a   Rico, M ^a   Angeles Jimenez M ^a  

^a INSTITUTO DE ESTRUCTURA DE LA MATERIA   (Spain)

Author keywords

NMR; Peptide design; Protein folding; Side chain interactions; hairpin; turn

Indexed keywords

AMINO ACID;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; CARBOXY TERMINAL SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE;

AMINO ACID SEQUENCE; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, CHEMICAL; MOLECULAR SEQUENCE DATA; PEPTIDE BIOSYNTHESIS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; WATER;

EID: 0034488879     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.11.2151     Document Type: Article

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