Proton NMR assignments and regular backbone structure of bovine pancreatic ribonuclease A in aqueous solution.
Proton NMR assignments and regular backbone structure of bovine pancreatic ribonuclease A in aqueous solution.
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水溶液中牛胰腺核糖核酸酶 A 的质子 NMR 归属和规则主链结构。
DOI：
10.1021/bi00440a033
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发表时间：
1989
期刊：
影响因子：
2.9
通讯作者：
Scheraga,HA
中科院分区：
文献类型：
--
作者：
Robertson,AD;Purisima,EO;Eastman,MA;Scheraga,HA
1989年3月29日摘要：对牛胰腺核糖核酸酶A（RNase A）的124个残基中的121个进行了质子NMR分配。在第一阶段的分配，COSY和中继COSY数据被用来确定属于丙氨酸，缬氨酸，苏氨酸，异亮氨酸和丝氨酸残基的40个氨基酸的自旋系统。还鉴定了大约60个其他NH-aCH-/3CH系统，但未分配到特定的氨基酸类型。然后，NOESY数据被用来连接顺序相邻的自旋系统;在RNase A中可能的700个共振中，大约有475个是以这种方式分配的。我们的分配与先前分配的20个残基的分配一致[Hahn，U.，& Riiterjans，H.（1985）Eur. J.Biochem.152，481-491]，另外的NOESY相关性用于鉴定RNA酶A中的规则骨架结构元件，其与X射线晶体学研究中观察到的那些非常相似[Wlodawer，A.，Borkakoti，N.，Moss，D.美国，& Howlin，B. 03 The Dog of the Woman（1986）B42，379-387]，^牛胰腺核糖核酸酶A（RNase A）1在蛋白质结构（Scheraga & Rupley，1962;理查兹&维科夫，1971）、折叠（Kim & Baldwin，1982）和酶催化（Blackburn &摩尔，1982）的研究中发挥了关键作用。我们建议通过使用核磁共振光谱来扩展这些研究，最近已经开始产生关于小蛋白质溶液结构的详细信息（Wiithrich，1986）。RNase A的NMR研究始于1957年，首次发表了蛋白质的1H NMR谱（Saunders
Revised Manuscript Received March 29, 1989 abstract: Proton NMR assignments have been made for 121 of the 124 residues of bovine pancreatic ribonuclease A (RNase A). During the first stage of assignment, COSY and relayed COSY data were used to identify 40 amino acid spin systems belonging to alanine, valine, threonine, isoleucine, and serine residues. Approximately 60 other NH-aCH-/3CH systems were also identified but not assigned to specific amino acid type. NOESY data then were used to connect sequentially neighboring spin systems; ap-proximately 475 of the possible 700 resonances in RNase A were assigned in this way. Our assignments agree with those for 20 residues assigned previously [Hahn, U., & Riiterjans, H.(1985) Eur. J. Biochem. 152, 481-491], Additional NOESY correlations were used to identify regularbackbone structure elements in RNase A, which are very similar to those observed in X-ray crystallographic studies [Wlodawer, A., Borkakoti, N., Moss, D. S., & Howlin, B.(1986) Acta Crystallogr. B42, 379-387],^ Bovine pancreatic ribonuclease A (RNase A) 1 has played a pivotal role in studies of protein structure (Scheraga & Rupley, 1962; Richards & Wyckoff, 1971), folding (Kim & Baldwin, 1982), and enzyme catalysis (Blackburn & Moore, 1982). We propose extending these studies through the use of NMR spectroscopy, which recently has begun to yield detailed information about the solution structure of small proteins (Wiithrich, 1986). NMR studies of RNase A date from 1957, with the pub-lication of the first'H NMR spectrum for a protein (Saunders