使用恒时演化对13C标记蛋白质进行改进的三维1H-13C-1H相关光谱分析。
Improved three-dimensional 1H-13C-1H correlation spectroscopy of a 13C-labeled protein using constant-time evolution.
作者信息
Ikura M, Kay L E, Bax A
机构信息
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
出版信息
J Biomol NMR. 1991 Sep;1(3):299-304. doi: 10.1007/BF01875522.
An improved version of the three-dimensional HCCH-COSY NMR experiment is described that correlates the resonances of geminal and vicinal proton pairs with the chemical shift of the 13C nucleus attached to one of the protons. The experiment uses constant-time evolution of transverse 13C magnetization which optimizes transfer of magnetization and thus improves the sensitivity of the experiment over the original scheme. The experiment is demonstrated for calmodulin complexed with a 26-residue peptide comprising the binding site of skeletal muscle myosin light chain kinase.
本文描述了一种改进的三维HCCH-COSY核磁共振实验，该实验将偕位和邻位质子对的共振与连接其中一个质子的13C核的化学位移相关联。该实验利用横向13C磁化的恒时演化，优化了磁化传递，从而提高了实验相对于原始方案的灵敏度。本文展示了该实验用于与包含骨骼肌肌球蛋白轻链激酶结合位点的26个残基肽复合的钙调蛋白。
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