Farrow N A, Zhang O, Forman-Kay J D, Kay L E
Protein Engineering Network Centres of Excellence, University of Toronto, ON, Canada.
J Biomol NMR. 1994 Sep;4(5):727-34. doi: 10.1007/BF00404280.
A heteronuclear correlation experiment is described which permits simultaneous characterization of both 15N longitudinal decay rates and slow conformational exchange rates. Data pertaining to the exchange between folded and unfolded forms of an SH3 domain is used to illustrate the technique. Because the unfolded form of the molecule, on average, shows significantly higher NH exchange rates than the folded form, an approach which minimizes the degree of water saturation is employed, enabling the extraction of accurate rate constants.
描述了一种异核相关实验，该实验允许同时表征15N纵向衰减率和缓慢的构象交换率。使用与SH3结构域的折叠和未折叠形式之间的交换有关的数据来说明该技术。由于分子的未折叠形式平均显示出比折叠形式明显更高的NH交换率，因此采用了一种使水饱和程度最小化的方法，从而能够提取准确的速率常数。
