通过核磁共振光谱学研究的蛋白质复合物。
Protein complexes studied by NMR spectroscopy.
作者信息
Wand A J, Englander S W
机构信息
Department of Biological Sciences, State University of New York at Buffalo 14260, USA.
出版信息
Curr Opin Biotechnol. 1996 Aug;7(4):403-8. doi: 10.1016/s0958-1669(96)80115-7.
Abstract
Recent advances in NMR methods now allow protein complexes to be studied in great detail in a wide range of solution conditions. Isotope-enrichment strategies, resonance-assignment approaches and structural-determination methods have evolved to the point where almost any type of complex involving proteins of reasonable size may be studied in a straightforward way. A variety of isotope editing and filtering strategies underlie these powerful methodologies. Approaches to the characterization of the dynamics of protein complexes have also matured to the point where detailed studies of the effects of complexation on dynamics can be studied over a wide range of timescales.
摘要
核磁共振（NMR）方法的最新进展使得在广泛的溶液条件下能够非常详细地研究蛋白质复合物。同位素富集策略、共振归属方法和结构测定方法已经发展到几乎可以直接研究涉及合理大小蛋白质的任何类型复合物的程度。这些强大方法的基础是多种同位素编辑和过滤策略。蛋白质复合物动力学表征方法也已成熟，能够在广泛的时间尺度上对复合物形成对动力学的影响进行详细研究。
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