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

Henrike Heise, Sorin M Luca, Bert L. De Groot, Helmut Grubmüller, Marc Baldus

Research output: Contribution to journalArticle

37 Citations (Scopus)

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 neu retransmitter transferred from a frozen aqueous solution via a lipid model phase to the receptor-bound form. The results speak against a conformational preorganization 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.

Original languageEnglish (US)
Pages (from-to)2113-2120
Number of pages8
JournalBiophysical Journal
Volume89
Issue number3
DOIs
StatePublished - Jan 1 2005

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Neurotensin
Molecular Dynamics Simulation
Peptides
Protein Folding
G-Protein-Coupled Receptors
Detergents
Ligands
Lipids

ASJC Scopus subject areas

  • Biophysics

Cite this

Probing conformational disorder in neurotensin by two-dimensional solid-state NMR and comparison to molecular dynamics simulations. / Heise, Henrike; Luca, Sorin M; De Groot, Bert L.; Grubmüller, Helmut; Baldus, Marc.

In: Biophysical Journal, Vol. 89, No. 3, 01.01.2005, p. 2113-2120.

Research output: Contribution to journalArticle

Heise, Henrike ; Luca, Sorin M ; De Groot, Bert L. ; Grubmüller, Helmut ; Baldus, Marc. / Probing conformational disorder in neurotensin by two-dimensional solid-state NMR and comparison to molecular dynamics simulations. In: Biophysical Journal. 2005 ; Vol. 89, No. 3. pp. 2113-2120.
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