The Ac-RGD-NH2 peptide as a probe of slow conformational exchange of short linear peptides in DMSO

Biopolymers

Volumn 69, Issue 1, 2003, Pages 72-86

  Biris, Nikolaos ^a   Stavrakoudis, Athanassios ^a   Politou, Anastasia S ^b   Mikros, Emmanuel ^c   Sakarellos Daitsiotis, Maria ^a   Sakarellos, Constantinos ^a   Tsikaris, Vassilios ^a  

^a UNIVERSITY OF IOANNINA   (Greece)

^b UNIVERSITY OF IOANNINA   (Greece)

^c UNIVERSITY OF ATHENS   (Greece)

Author keywords

Arginine ionic interactions; Aspartic acid ionic interactions; Fibrinogen inhibitor; Hydrogen bonds; NMR; Peptide folding; RGD peptide; Slow conformational exchange

Indexed keywords

CONFORMATIONS; DISSOLUTION; HYDROGEN BONDS; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; THERMAL EFFECTS;

CHEMICAL SHIFTS; PEPTIDES;

BIOPOLYMERS;

ARGINYLGLYCYLASPARTIC ACID; DIMETHYL SULFOXIDE; PEPTIDE DERIVATIVE; ARGINYL-GLYCYL-ASPARTIC ACID; OLIGOPEPTIDE; WATER;

ARTICLE; CONFORMATIONAL TRANSITION; ENVIRONMENTAL TEMPERATURE; HIGH TEMPERATURE; HYDROGEN BOND; LOW TEMPERATURE; MOLECULE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE ANALYSIS; PEPTIDE SYNTHESIS; PROTEIN CONFORMATION; ROOM TEMPERATURE; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; PH; SOLUTION AND SOLUBILITY; STRUCTURE ACTIVITY RELATION; THERMODYNAMICS;

AMINO ACID SEQUENCE; DIMETHYL SULFOXIDE; HYDROGEN-ION CONCENTRATION; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; OLIGOPEPTIDES; PROTEIN CONFORMATION; SOLUTIONS; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS; WATER;

EID: 0038713285     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/bip.10335     Document Type: Article

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