Residual dipolar couplings in short peptidic foldamers: Combined analyses of backbone and side-chain conformations and evaluation of structure coordinates of rigid unnatural amino acids

ChemBioChem

Volumn 10, Issue 3, 2009, Pages 440-444

  Schmid, Markus B ^a   Fleischmann, Matthias ^a   D'Elia, Valerio ^a   Reiser, Oliver ^a   Gronwald, Wolfram ^a   Gschwind, Ruth M ^a  

^a UNIVERSITY OF REGENSBURG   (Germany)

Author keywords

Conformation analysis; NMR spectroscopy; Peptides; Peptidic foldamers; Residual dipolar couplings; Unnatural amino acids

Indexed keywords

AMINO ACID; CYSTEINE; INTEGRIN; NEUROPEPTIDE Y; PROLINE;

AMINO ACID ANALYSIS; ARTICLE; COMPUTER SIMULATION; CONFORMATIONAL TRANSITION; GENETIC LINKAGE; MOLECULAR DYNAMICS; MOLECULAR MODEL; MOLECULAR PROBE; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTON NUCLEAR MAGNETIC RESONANCE; QUALITATIVE ANALYSIS; STRUCTURE ACTIVITY RELATION;

AMINO ACIDS; MOLECULAR CONFORMATION; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PROTEIN FOLDING;

EID: 60349099238     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.200800736     Document Type: Article

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