Disorder and order in unfolded and disordered peptides and proteins: A view derived from tripeptide conformational analysis. I. Tripeptides with long and predominantly hydrophobic side chains

Proteins: Structure, Function and Bioinformatics

Volumn 81, Issue 6, 2013, Pages 955-967

  Schweitzer Stenner, Reinhard ^a   Hagarman, Andrew ^b   Toal, Siobhan ^a   Mathieu, Daniel ^c   Schwalbe, Harald ^c  

^a DREXEL UNIVERSITY   (United States)

^b DUKE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c GOETHE UNIVERSITY   (Germany)

Author keywords

Coil library distributions; Conformational distributions; J coupling constants; Tripeptides; Unfolded state of proteins and peptides; Vibrational and NMR spectroscopy

Indexed keywords

AMINO ACID; GLYCYLLEVO ARGINYLGLYCINE; GLYCYLLEVO ISOLEUCYLGLYCINE; GLYCYLLEVO TYROSYLGLYCINE; POLYPEPTIDE; TRIPEPTIDE; UNCLASSIFIED DRUG;

AQUEOUS SOLUTION; ARTICLE; COMPARATIVE STUDY; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION;

HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MOLECULAR CONFORMATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OLIGOPEPTIDES; PROTEIN STRUCTURE, SECONDARY; PROTEIN UNFOLDING;

EID: 84878147471     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24225     Document Type: Article

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