Determination of protein structures in the solid state from NMR chemical shifts

Paul Robustelli; Andrea Cavalli; Michele Vendruscolo

doi:10.1016/j.str.2008.10.016

Determination of protein structures in the solid state from NMR chemical shifts

Structure. 2008 Dec 10;16(12):1764-9. doi: 10.1016/j.str.2008.10.016.

Authors

Paul Robustelli¹, Andrea Cavalli, Michele Vendruscolo

Affiliation

¹ Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.

PMID: 19081052
DOI: 10.1016/j.str.2008.10.016

Abstract

Solid-state NMR spectroscopy does not require proteins to form crystalline or soluble samples and can thus be applied under a variety of conditions, including precipitates, gels, and microcrystals. It has recently been shown that NMR chemical shifts can be used to determine the structures of the native states of proteins in solution. By considering the cases of two proteins, GB1 and SH3, we provide an initial demonstration here that this type of approach can be extended to the use of solid-state NMR chemical shifts to obtain protein structures in the solid state without the need for measuring interatomic distances.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacterial Proteins / chemistry
Crystallization
Models, Chemical
Models, Molecular
Nuclear Magnetic Resonance, Biomolecular / methods*
Protein Conformation
Protein Structure, Secondary
Proteins / chemistry*
X-Ray Diffraction
src Homology Domains

Substances

Bacterial Proteins
Proteins