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|
|Link:||<Go to ISI>://A1992JW79700041|
|Publisher:||American Chemical Society|
|Appears in Collections:||Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)|
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