Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 21, Issue 4, Pages 497-508Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2011.06.009
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Funding
- BBSRC [BB/G011915/1]
- BBSRC [BB/E013228/1, BB/G011915/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/G011915/1, BB/E013228/1] Funding Source: researchfish
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NMR spectroscopy has established itself as one of the main techniques for the structural study of integral membrane proteins. Remarkably, over the last few years, substantial progress has been achieved in the structure determination of increasingly complex polytopical alpha-helical membrane proteins, with their size approaching similar to 100 kDa. Such advances are the result of significant improvements in NMR methodology, sample preparation and powerful selective isotope labelling schemes. We review the requirements facilitating such work based on the more recent solution NMR studies of alpha-helical proteins. While the majority of such studies still use detergent-solubilized proteins, alternative more native-like lipid-based media are emerging. Recent interaction, dynamics and conformational studies are discussed that cast a promising light on the future role of NMR in this important and exciting area.
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