NMR Detection of Bifurcated Hydrogen Bonds in Large Proteins

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• 作者：Aizhuo Liu ; Zhenwei Lu ; Jifeng Wang ; Lishan Yao ; Yue Li ; Honggao Yan
• 刊名：Journal of the American Chemical Society
• 出版年：2008
• 出版时间：February 27, 2008
• 年：2008
• 卷：130
• 期：8
• 页码：2428 - 2429
• 全文大小：44K
• 年卷期：v.130,no.8(February 27, 2008)
• ISSN：1520-5126

文摘

Hydrogen bonds play critical roles in protein structure, stability, and function. Conventionally, hydrogen bonds are mainly determined by X-ray crystallography and NOE-based NMR spectroscopy in indirect manners. In recent years, it was demonstrated that hydrogen bonds can be directly detected through NMR measurements of trans-hydrogen-bond scalar coupling constants. Here we report across hydrogen-bond protium/deuterium isotope effects in a 35 kDA protein observed with the isotopomer-selective TROSY NMR technique (Liu et al. J. Biomol. NMR 2006, 36, 205-214; Liu et al. J. Magn. Reson. 2007, 186, 319-326) and show that such isotope effects can be used to detect a most common type of bifurcated hydrogen bonds, in which a heavy atom, usually oxygen, is involved in two hydrogen bonds, including a pair of bifurcated hydrogen bonds involving a bound water molecule.