Modulation of intrinsic phi,psi propensities of amino acids by neighbouring residues in the coil regions of protein structures: NMR analysis and dissection of a beta-hairpin peptide

Analysis of residues in coil regions of protein structures presents a novel approach to deconvoluting the various competing factors which determine the intrinsic phi,psi propensities of amino acids free from the regular interactions associated with beta-strands and alpha-helices. We have considered...

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Veröffentlicht in:	Journal of molecular biology 1998-12, Vol.284 (5), p.1597-1609
Hauptverfasser:	Griffiths-Jones, S R, Sharman, G J, Maynard, A J, Searle, M S
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino Acids - chemistry Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Peptides - chemistry Protein Conformation Protein Folding Protein Structure, Secondary Proteins - chemistry Water
Online-Zugang:	Volltext
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