Long-distance effects of site-directed mutations on backbone conformation in bacteriorhodopsin from solid state NMR of [1-13C]Val-labeled proteins.

We have recorded 13C cross-polarization-magic angle spinning and dipolar decoupled-magic angle spinning NMR spectra of [1-13C]Val-labeled wild-type bacteriorhodopsin (bR), and the V49A, V199A, T46V, T46V/V49A, D96N, and D85N mutants, in order to study conformational changes of the backbone caused by...

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Bibliographic Details
Main Authors: Tanio, M, Inoue, S, Yokota, K, Seki, T, Tuzi, S, Needleman, R, Lanyi, J K, Naito, A, Saitô, H
Format: Artigo
Language:Inglês
Published: 1999
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Research Article
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC1300341/
https://ncbi.nlm.nih.gov/pubmed/10388769
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