Protein dynamics studied by rotating frame 15N spin relaxation times
Protein dynamics studied by rotating frame 15N spin relaxation times
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通过旋转框架 15N 自旋弛豫时间研究蛋白质动力学
DOI：
10.1007/bf00178259
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发表时间：
1993
影响因子：
2.7
通讯作者：
K. Wüthrich
中科院分区：
文献类型：
--
作者：
T. Szyperski;P. Luginbühl;G. Otting;P. Güntert;K. Wüthrich
摘要 通过测量骨架 15N 自旋的旋转框架弛豫时间作为自旋锁功率的函数，研究了 36°C 下均匀 15N 标记的胰腺胰蛋白酶抑制剂 (BPTI) 水溶液中的构象速率过程。确定了两种不同的分子内交换过程。第一个局部速率过程涉及残基Cys38和Arg39，相关时间约为1.3毫秒，并且与二硫键Cys14-Cys38的手性异构化有关。第二种更快的运动模式叠加在二硫键异构化上，并暂时归因于多肽序列-Cys14-Ala15-Lys16-中的局部片段运动。假设弛豫主要由偶极耦合和各向同性分子重新取向调节的化学位移各向异性主导，则发现蛋白质整体旋转翻滚的相关时间为 2 ns。
SummaryConformational rate processes in aqueous solutions of uniformly 15N-labeled pancreatic trypsin inhibitor (BPTI) at 36°C were investigated by measuring the rotating frame relaxation times of the backbone 15N spins as a function of the spin-lock power. Two different intramolecular exchange processes were identified. A first local rate process involved the residues Cys38 and Arg39, had a correlation time of about 1.3 ms, and was related to isomerization of the chirality of the disulfide bond Cys14-Cys38. A second, faster motional mode was superimposed on the disulfide bond isomerization and was tentatively attributed to local segmental motions in the polypeptide sequence-Cys14-Ala15-Lys16-. The correlation time for the overall rotational tumbling of the protein was found to be 2 ns, using the assumption that relaxation is dominated by dipolar coupling and chemical shift anistropy modulated by isotropic molecular reorientation.
通过 15N NMR 弛豫测量确定枯草芽孢杆菌葡萄糖通透酶 IIA 结构域的骨架动力学。
影响因子：
2.9
作者：
Stone,MJ;Fairbrother,WJ;Palmer3rd,AG;Reizer,J;SaierJr,MH;Wright,PE
通讯作者：
Wright,PE
通过二维质子检测 15N NMR 光谱研究负载钙的钙结合蛋白 D9k 的主链动力学。
影响因子：
2.9
作者：
Kördel,J;Skelton,NJ;Akke,M;Palmer3rd,AG;Chazin,WJ
通讯作者：
Chazin,WJ
影响因子：
2.9
作者：
SCHNEIDER, DM;DELLWO, MJ;WAND, AJ
通讯作者：
WAND, AJ