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Proton evolved local field solid-state nuclear magnetic resonance using Hadamard encoding: theory and application to membrane proteins. J Chem Phys 2011 Aug 21;135(7):074503

Date

08/25/2011

Pubmed ID

21861572

Pubmed Central ID

PMC3172034

DOI

10.1063/1.3622604

Scopus ID

2-s2.0-80052049670 (requires institutional sign-in at Scopus site)   16 Citations

Abstract

NMR anisotropic parameters such as dipolar couplings and chemical shifts are central to structure and orientation determination of aligned membrane proteins and liquid crystals. Among the separated local field experiments, the proton evolved local field (PELF) scheme is particularly suitable to measure dynamically averaged dipolar couplings and give information on local molecular motions. However, the PELF experiment requires the acquisition of several 2D datasets at different mixing times to optimize the sensitivity for the complete range of dipolar couplings of the resonances in the spectrum. Here, we propose a new PELF experiment that takes the advantage of the Hadamard encoding (HE) to obtain higher sensitivity for a broad range of dipolar couplings using a single 2D experiment. The HE scheme is obtained by selecting the spin operators with phase switching of hard pulses. This approach enables one to detect four spin operators, simultaneously, which can be processed into two 2D spectra covering a broader range of dipolar couplings. The advantages of the new approach are illustrated for a U-(15)N NAL single crystal and the U-(15)N labeled single-pass membrane protein sarcolipin reconstituted in oriented lipid bicelles. The HE-PELF scheme can be implemented in other multidimensional experiments to speed up the characterization of the structure and dynamics of oriented membrane proteins and liquid crystalline samples.

Author List

Gopinath T, Mote KR, Veglia G

Author

Gopinath Tata PhD Assistant Professor in the Biophysics department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Escherichia coli
Membrane Proteins
Muscle Proteins
Nuclear Magnetic Resonance, Biomolecular
Proteolipids
Protons
Recombinant Fusion Proteins