Coastal photograph: Aber Wrac'h, Pays du Léon, Bretagne

Aber Wrac’h, Pays du Léon, Bretagne. Aber Wrac’h, Bretagne, France, on 10 March 2004 at 13:30 (low tide) looking North (downstream) towards the Aber mouth and open sea between Lannilis and Plougerneau, Pays des Abers, Pays du Le´on. The word "Aber" is Britton (Breton) for a "fjord"-like estuary. Located on the Channel, the region "Pays des Abers" includes several deep incisions in the coastlines. The best known ‘‘Abers’’ are the Aber Wrac’h and Aber Benoit in the Pays du Léon, Finistere Nord.

Conformational analysis of LYS(11-36), a peptide derived from the beta-sheet region of T4 lysozyme, in TFE and SDS

The solution conformation of a peptide LYS(11-36), which corresponds to the beta-sheet region in T4 lysozyme, has been examined in aqueous solution, TFE, and SDS micelles by CD and H-1 NMR spectroscopy. Secondary structure predictions suggest some beta-sheet and turn character in aqueous solution but predict a helical conformation in a more hydrophobic environment. The predictions were supported by the CD and NMR studies which showed the peptide to be relatively unstructured in aqueous solution, although there was some evidence of a beta-turn conformer which was maintained in 200 mM SDS and, to a lesser extent, in 50% TFE. The peptide was significantly helical in the presence of either 50% TFE or 200 mM SDS. TFE and SDS titrations showed that the peptide could form helical, sheet, or extended structure depending on the TFE or SDS concentration. The studies indicate that peptide environment is the determining factor in secondary structure adopted by LYS(11-36).