Journal
JOURNAL OF MAGNETIC RESONANCE
Volume 178, Issue 1, Pages 162-165Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jmr.2005.08.008
Keywords
solid-state NMR; aligned sample; phospholipid bilayer; membrane protein; rotational diffusion
Funding
- NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING [P41EB002031] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [F32GM066487, R01GM066978, P01GM064676] Funding Source: NIH RePORTER
- NIBIB NIH HHS [P41EB002031] Funding Source: Medline
- NIGMS NIH HHS [F32GM655833, F32GM66487, P01GM064676, R01GM066978] Funding Source: Medline
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Solid-state NMR experiments on mechanically aligned bilayer and magnetically aligned bicelle samples demonstrate that membrane proteins undergo rapid rotational diffusion about the normal in phospholipid bilayers. Narrow single-line resonances are observed from N-15 labeled sites in the trans-membrane helix of the channel-forming domain of the protein Vpu from HIV-1 in phospholipid bilayers with their normals at angles of 0 degrees, 20 degrees, 40 degrees, and 90 degrees, and bicelles with their normals at angles of 0 degrees and 90 degrees with respect to the direction of the applied magnetic field. This could only occur if the entire polypeptide undergoes rotational diffusion about the bilayer normal. Comparisons between experimental and simulated spectra are consistent with a rotational diffusion coefficient (D-R) of approximately 10(5) s(-1). (c) 2005 Published by Elsevier Inc.
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