Significance of Bound Residual Water in the Dmso Solution Structure of Stable Peptide Hydrates (Journal article)

Tsikaris, V./ Sakarellos-Daitsiotis, M./ Theophanidis, N./ Sakarellos, C./ Cung, M. T./ Marraud, M.

Water molecules in peptide hydrates are widely known to be directly involved in the stabilization of the peptide structure in the solid state. In this work, the influence of tightly bound residual water molecules on the conformational properties of two hydrates of the L-Arg-L-Leu-Gly and Gly-L-Phe-L-Leu peptide lyophilized from water at acidic pH, has been investigated for the first time in DMSO solution by means of 1D and 2D H-1 NMR spectroscopy. Significant conformational changes have been observed in solution as the bound residual water is gradually expelled from the peptide hydrate. These observations point out the crucial role of bound water in fine-structural determinations of peptides in solution when evaluating NMR data.
Institution and School/Department of submitter: Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας
Keywords: sequential polypeptides,protein hydration,organic-solvents,aqueous-solution,histone models,enkephalin,crystal,conformation,spectroscopy,resolution
ISSN: 0300-9580
Link: <Go to ISI>://A1991GF28500006
Publisher: The Royal Society of Chemistry
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

Files in This Item:
There are no files associated with this item.

 Please use this identifier to cite or link to this item:
  This item is a favorite for 0 people.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.