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

Abstract:

:It has recently been reported that synthetic peptides corresponding to the C-terminal sequence of G alpha, 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 G alpha(S) C-terminus, G alpha(S)(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 alpha-turn and a type III beta-turn involving the last five C-terminal residues. Interestingly, the alpha-turn conformation was found to overlap with good agreement the crystallographic structure of the same fragment in the G alpha(S) protein.

journal_name

Biopolymers

journal_title

Biopolymers

authors

Albrizio S,D'Ursi A,Fattorusso C,Galoppini C,Greco G,Mazzoni MR,Novellino E,Rovero P

doi

10.1002/1097-0282(200009)54:3<186::AID-BIP50>3.0.C

subject

Has Abstract

pub_date

2000-09-01 00:00:00

pages

186-94

issue

3

eissn

0006-3525

issn

1097-0282

pii

10.1002/1097-0282(200009)54:3<186::AID-BIP50>3.0.C

journal_volume

54

pub_type

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