Peptide T exhibits a well-defined structure in fluorinated solvent at low temperature.

Autor: Yang TC; Department of Biochemistry, Memorial University of Newfoundland, St. John's, NL, Canada., Rendell J, Gulliver W, Booth V
Jazyk: angličtina
Zdroj: Journal of peptide science : an official publication of the European Peptide Society [J Pept Sci] 2009 Dec; Vol. 15 (12), pp. 818-23.
DOI: 10.1002/psc.1179
Abstrakt: The structure of Peptide T was determined by solution NMR spectroscopy, under strong structure-inducing conditions: 40% hexafluoro-2-propanol aqueous solution at 5 degrees C. Under these conditions it was possible to detect medium-range NOEs for the first time for this peptide. This allowed a much better-defined structure to be determined for Peptide T in comparison with earlier NMR and computational studies. Peptide structures consistent with the experimental restraints were generated using a restrained MD simulation with a full empirical force field. Residues 4-8 of Peptide T take on a well-defined structure with a heavy atom RMSD of 0.78 A. The structure is stabilized by hydrogen bonding to side-chain oxygen atoms of Thr 4 and Thr 8, as well as backbone hydrogen bonding between residues 5 and 7 that forms this region into a classic gamma-turn.
((c) 2009 European Peptide Society and John Wiley & Sons, Ltd.)
Databáze: MEDLINE
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