Folding of a β-hairpin peptide derived from the N-terminus of ubiquitin: Conformational preferences of β-turn residues dictate non-native β-strand interactions

European Journal of Biochemistry

Volumn 267, Issue 12, 2000, Pages 3539-3548

  Jourdan, Muriel ^b   Griffiths Jones, Samuel R ^b   Searle, Mark S ^a  

^a UNIVERSITY OF NOTTINGHAM   (United Kingdom)

^b NONE

Author keywords

turn ; hairpin peptide; Circular dichroism spectroscopy; NMR spectroscopy; Protein folding

Indexed keywords

UBIQUITIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CIRCULAR DICHROISM; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING;

AMINO ACID SEQUENCE; DATABASES, FACTUAL; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN FOLDING; SOLUTIONS; UBIQUITINS;

EID: 0000901301     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01381.x     Document Type: Article

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