Probing conformational disorder in neurotensin by two-dimensional solid-state NMR and comparison to molecular dynamics simulations.

Abstract:

:An approach is introduced to characterize conformational ensembles of intrinsically unstructured peptides on the atomic level using two-dimensional solid-state NMR data and their combination with molecular dynamics simulations. For neurotensin, a peptide that binds with high affinity to a G-protein coupled receptor, this method permits the investigation of the changes in conformational preferences of a neurotransmitter transferred from a frozen aqueous solution via a lipid model phase to the receptor-bound form. The results speak against a conformational pre-organization of the ligand in detergents in which the receptor has been shown to be functional. Further extensions to the study of protein folding are possible.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Heise H,Luca S,de Groot BL,Grubmüller H,Baldus M

doi

10.1529/biophysj.105.059964

subject

Has Abstract

pub_date

2005-09-01 00:00:00

pages

2113-20

issue

3

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(05)72855-1

journal_volume

89

pub_type

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