It has recently been reported that synthetic peptides corresponding to the C-terminal sequence of G, can be used to study the molecular mechanisms of interaction between this protein and G protein coupled receptors (Hamm et al., Science, 1988, Vol. 241, pp. 832-835). A conformational analysis on a 11 amino acids peptide from the GS C-terminus, GS(384-394) (H-QRMHLRQYELL-OH), was performed by nmr spectroscopy and molecular modeling methods. Two-dimensional nmr spectra, recorded in hexafluoroacetone/water, a mixture with structure stabilizing properties, showed an unusually high number of nuclear Overhauser effects, forming significative pattern to the drawing of a secondary structure. Conformations consistent with experimental NOE distances were obtained through molecular dynamics and energy minimization methods. These calculations yielded two stable conformers corresponding to an -turn and a type III -turn involving the last five C-terminal residues. Interestingly, the -turn conformation was found to overlap with good agreement the crystallographic structure of the same fragment in the GS protein.

Conformational studies on a synthetic C-terminal fragment of the alpha subunit of G(S) proteins / Albrizio, Stefania; D'Ursi, A. M.; Fattorusso, Caterina; Galoppini, C.; Greco, Giovanni; Mazzoni, M. R.; Novellino, Ettore; Rovero, P.. - In: BIOPOLYMERS. - ISSN 0006-3525. - STAMPA. - 54:(2000), pp. 186-194. [10.1002/1097-0282(200009)54:3<186::AID-BIP50>3.0.CO;2-2]

Conformational studies on a synthetic C-terminal fragment of the alpha subunit of G(S) proteins.

ALBRIZIO, STEFANIA;FATTORUSSO, CATERINA;GRECO, GIOVANNI;NOVELLINO, ETTORE
;
2000

Abstract

It has recently been reported that synthetic peptides corresponding to the C-terminal sequence of G, can be used to study the molecular mechanisms of interaction between this protein and G protein coupled receptors (Hamm et al., Science, 1988, Vol. 241, pp. 832-835). A conformational analysis on a 11 amino acids peptide from the GS C-terminus, GS(384-394) (H-QRMHLRQYELL-OH), was performed by nmr spectroscopy and molecular modeling methods. Two-dimensional nmr spectra, recorded in hexafluoroacetone/water, a mixture with structure stabilizing properties, showed an unusually high number of nuclear Overhauser effects, forming significative pattern to the drawing of a secondary structure. Conformations consistent with experimental NOE distances were obtained through molecular dynamics and energy minimization methods. These calculations yielded two stable conformers corresponding to an -turn and a type III -turn involving the last five C-terminal residues. Interestingly, the -turn conformation was found to overlap with good agreement the crystallographic structure of the same fragment in the GS protein.
2000
Conformational studies on a synthetic C-terminal fragment of the alpha subunit of G(S) proteins / Albrizio, Stefania; D'Ursi, A. M.; Fattorusso, Caterina; Galoppini, C.; Greco, Giovanni; Mazzoni, M. R.; Novellino, Ettore; Rovero, P.. - In: BIOPOLYMERS. - ISSN 0006-3525. - STAMPA. - 54:(2000), pp. 186-194. [10.1002/1097-0282(200009)54:3<186::AID-BIP50>3.0.CO;2-2]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/147168
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