Influence of conformation on the fluorescence of tryptophan-containing peptides

✍ Scribed by Janet S. Anderson; Gary S. Bowitch; Robert L. Brewster

• Book ID: 102763616
• Publisher: Wiley (John Wiley & Sons)
• Year: 1983
• Tongue: English
• Weight: 1004 KB
• Volume: 22
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.360221111

✦ Synopsis

done using an empirical energy program for peptides (ECEPP). The resulting low-energy conformations were analyzed for the presence of hydrogen bonds, the distances between carbonyl groups and the indole ring, the distances between the N-terminal amino group and the indole ring, the dihedral angle between the planes containing carbonyl groups and the indole ring, and for dipeptides with two aromatic side chains, the dihedral angle and distance between the planes of the aromatic rings. This information was correlated with literature data from x-ray crystallographic studies, fluorescence lifetime studies, and quantum-yield experiments; proposed models of intramolecular quenching are discussed in light of the peptide conformations.