Bycroft M, Sheppard R N, Lau F T, Fersht A R
MRC Unit for Protein Function and Design, University Chemical Laboratory, Cambridge, U.K.
Biochemistry. 1990 Aug 14;29(32):7425-32. doi: 10.1021/bi00484a011.
Two-dimensional nuclear magnetic resonance spectroscopy has been used to study the bacterial ribonuclease barnase (MW 12,382). Resonance assignments have been made for protons in all of the 110 residues. Analysis of medium- and long-range contacts in NOESY spectra has demonstrated that the major elements of secondary structure in barnase in solution are essentially identical with those found in the crystal structure.
二维核磁共振光谱已被用于研究细菌核糖核酸酶巴纳酶(分子量12,382)。已对所有110个残基中的质子进行了共振归属。对NOESY谱中的中程和远程接触的分析表明,溶液中巴纳酶的二级结构主要元素与晶体结构中的基本相同。