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Originally published as Biophys J. BioFAST on July 1, 2005.
doi:10.1529/biophysj.105.059964
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Biophysical Journal 89:2113-2120 (2005)
© 2005 The Biophysical Society

Probing Conformational Disorder in Neurotensin by Two-Dimensional Solid-State NMR and Comparison to Molecular Dynamics Simulations

Henrike Heise *, Sorin Luca *, Bert L. de Groot {dagger}, Helmut Grubmüller {dagger} and Marc Baldus *

* Department of NMR-Based Structural Biology and {dagger} Department of Theoretical and Computational Biophysics, Max-Planck-Institute for Biophysical Chemistry, 37077 Göttingen, Germany

Correspondence: Address reprint requests to Marc Baldus, Tel.: 49-551-201-2212; Fax: 49-551201-2202; E-mail: maba{at}mpibpc.mpg.de.

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 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.




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Copyright © 2005 by the Biophysical Society.