Solvation State of the Tyr Side-Chain in Peptides - an Ft-Ir and O-17 Nmr Approach (Journal article)

Gerothanassis, I. P./ Birlirakis, N./ Sakarellos, C./ Marraud, M.

Detailed studies of the O-17 NMR chemical shifts of the COH group of p-cresol and tyrosine derivatives as a function of pH and in a variety of solvents revealed an unusually large titration shift upon the deprotonation of the phenol group and a very small chemical shift variation as a function of solvent hydrogen-bonding ability. Similarly the nu(CO) stretching frequencies exhibit a very small variation as a function of solvent hydrogen-bonding ability, and discrete hydrogen-bonded species could not be identified. In contrast, the in-plane COH bending frequencies of these compounds have been shown to be very sensitive to hydrogen-bond interactions, and discrete hydrogen-bonded species could be identified. The applicability of this novel methodology to peptide hormones is demonstrated in the case of Leu-enkephalin in aqueous solution.
Institution and School/Department of submitter: Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας
Keywords: protein amino-acids,aqueous-solution,organic solution,enkephalin,tyrosine,bacteriorhodopsin,spectroscopy,polypeptides,morphine,spectra
ISSN: 0002-7863
Link: <Go to ISI>://A1992JW79700041
Publisher: American Chemical Society
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

Files in This Item:
File Description SizeFormat 
Gerothanassis-1992-Solvation State of t.pdf625.3 kBAdobe PDFView/Open    Request a copy

 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.