Arg side-chain-backbone interactions evidenced in model peptides by O-17-NMR spectroscopy

 
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2000 (EN)
Arg side-chain-backbone interactions evidenced in model peptides by O-17-NMR spectroscopy (EN)

Tsikaris, V. (EN)

Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας (EL)
Tsikaris, V. (EN)

The guanidinium group of arginine possesses a variety of biochemical functions, either by participating in direct interactions in recognition processes, or by stabilizing secondary structures. Three model compounds, selectively O-17 enriched, Ac-Arg-Ala-[O-17]Pro-NH2 (1), Piv-Arg-Pro-[O-17]Gly-NH2 (2) (C-terminal segment of the luteinizing hormone releasing hormone), and Piv-Nle-Pro-[O-17]Gly-NH2 (3), were prepared and studied by O-17-nmr spectroscopy. A direct hydrogen-bonded interaction between the Arg side chain and the carbonyl main chain carboxy-terminus was found, thus confirming the tendency of Arg to participate in proton-acceptor functions. (C) 2000 John Wiley & Sons, Inc. (EN)

o-17 hydrogen bonding (EN)

Πανεπιστήμιο Ιωαννίνων (EL)
University of Ioannina (EN)

Biopolymers (EN)

English

2000

<Go to ISI>://000084994700003

Wiley (EN)



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