Recent Developments in Biomolecular NMR
Recent Developments in Biomolecular NMR
复制标题
生物分子核磁共振的最新进展
DOI:
10.1039/9781849735391-00271
复制
发表时间:
2012
期刊:
影响因子:
--
通讯作者:
Bostock M
中科院分区:
文献类型:
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作者:
Bostock M
Membrane proteins are predicted to make up approximately one-third of proteins in the genome, 1 however, to date they remain significantly structurally under-represented, with unique structures comprising only 0.4% of all PDB-deposited structures. 2, 3 Nevertheless these figures must be set against a recent surge in structures of membrane proteins, including mammalian proteins, 4 following a predicted exponential trend. 5, 6 Whilst many of these structures have been solved by X-ray crystallography, NMR has also contributed a significant number, 7 currently 16%. 8 Considerable progress has also been made in the field of solid-state NMR, 9–11 however, in this review we focus on solution-state NMR. In particular, a number of recent structures demonstrate that solution NMR is able to tackle a range of large membrane proteins up to around y100 kDa. b-Barrel proteins12–15 remain easier to study because their secondary structure allows orientational information to be obtained through hydrogen bonds and short-range NOEs between adjacent strands. Recently, NMR has also proved able to study a range of large a-helical membrane proteins, 16–19 demonstrating that the technology has matured to a level at which membrane protein structure determination by NMR can be considered a viable approach.