Prospects for NMR of large proteins
Prospects for NMR of large proteins
复制标题
大蛋白质核磁共振的前景
DOI：
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发表时间：
1993
影响因子：
2.7
通讯作者：
G. Wagner
中科院分区：
文献类型：
--
作者：
G. Wagner
摘要在过去十年中，许多小蛋白质的溶液结构已通过核磁共振解析。核磁共振分析的蛋白质大小似乎在稳步增加。迄今为止，高达 18 kD 的蛋白质结构已被解析，并且高达 30 kD 的蛋白质光谱已被分配。因此，核磁共振成为一种有吸引力的技术，特别是对于无法结晶的蛋白质的结构研究。然而，该技术的应用受到蛋白质松弛特性的限制。如果弛豫仅通过斯托克斯-爱因斯坦型旋转扩散来确定，则可以容易地估计分子大小对蛋白质弛豫特性的影响，从而对多维多重共振实验的性能的影响。从这个角度来看，解决两倍或三倍更大的结构似乎是可能的。然而，大多数较大的蛋白质由于聚集或其他仍未知的影响而表现出严重的谱线加宽。目前，大蛋白质研究中面临的挑战是通过样品调节来最大程度地减少这些影响。
SummaryDuring the last decade, solution structures of many small proteins have been solved by NMR. The size of proteins that are being analyzed by NMR seems to increase steadily. Protein structures up to 18 kD have been solved sofar, and spectra of proteins up to 30 kD have been assigned. Thus, NMR emerges as an attractive technique, in particular for structural studies of proteins that cannot by crystallized. However, the application of the technology is limited by relaxation properties of the proteins. If relaxation would only be determined by Stokes-Einstein-type rotational diffusion, the effects of the molecular size on relaxation properties of proteins and thus on the performance of multi-dimensional multiple-resonance experiments could readily be estimated. From this perspective, solving two- or three-fold larger structures seems possible. However, most larger proteins exhibit serious line broadening due to aggregation or other still unknown effects. Sample conditioning to minimize these effects is presently the challenge in the work with large proteins.
影响因子：
2.9
作者：
PENG, JW;WAGNER, G
通讯作者：
WAGNER, G
溶液中人二氢叶酸还原酶的序列特异性 1H 和 15N 共振分配。
影响因子：
2.9
作者：
Stockman,BJ;Nirmala,NR;Wagner,G;Delcamp,TJ;DeYarman,MT;Freisheim,JH
通讯作者：
Freisheim,JH
影响因子：
2.9
作者：
LEMASTER, DM;RICHARDS, FM
通讯作者：
RICHARDS, FM