通过核磁共振光谱法鉴定葡萄球菌β-内酰胺酶展开过程中的一种稳定中间结构。
Identification by n.m.r. spectroscopy of a stable intermediate structure in the unfolding of staphylococcal beta-lactamase.
作者信息
Thomas R M, Feeney J, Nicholson R B, Pain R H, Roberts G C
出版信息
Biochem J. 1983 Dec 1;215(3):525-9. doi: 10.1042/bj2150525.
Abstract
The unfolding of beta-lactamase (penicillinase) from Staphylococcus aureus by guanidinium chloride was followed by using n.m.r. spectroscopy. On the basis of the observation of resonances corresponding to histidine, tyrosine and other amino acid side chains, the existence of a stable partially folded species was demonstrated. These experiments provide detailed characterization of the intermediate that confirms and extends previous characterization by absorption and c.d. spectroscopy and by flow properties. In addition, they show that residues in the N-terminal third of the molecule are affected by the native-to-intermediate transition. Persistent non-equivalence of the two imidazole C2 proton resonances at high guanidinium chloride concentrations is discussed in terms of local sequence effects on the chemical shift.
摘要
利用核磁共振光谱法跟踪了金黄色葡萄球菌β-内酰胺酶（青霉素酶）在氯化胍作用下的去折叠过程。基于对对应于组氨酸、酪氨酸和其他氨基酸侧链的共振的观察，证实了稳定的部分折叠物种的存在。这些实验提供了该中间体的详细特征，证实并扩展了先前通过吸收光谱、圆二色光谱和流动性质所做的表征。此外，实验表明分子N端三分之一区域的残基受天然态到中间体转变的影响。针对高氯化胍浓度下两个咪唑C2质子共振持续不等价的现象，从局部序列对化学位移的影响方面进行了讨论。
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本文引用的文献
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