Solution structure of murine epidermal growth factor: determination of the polypeptide backbone chain-fold by nuclear magnetic resonance and distance geometry.
Solution structure of murine epidermal growth factor: determination of the polypeptide backbone chain-fold by nuclear magnetic resonance and distance geometry.
复制标题
鼠表皮生长因子的溶液结构：通过核磁共振和距离几何测定多肽主链折叠。
DOI：
10.1073/pnas.84.15.5226
复制
发表时间：
1987
影响因子：
11.1
通讯作者：
Scheraga,HA
中科院分区：
文献类型：
--
作者：
Montelione,GT;Wüthrich,K;Nice,EC;Burgess,AW;Scheraga,HA
通过核磁共振波谱和距离几何计算确定了鼠表皮生长因子溶液结构中的多肽主链折叠。第333章 距离和二面角约束这些是通过核奥沃豪塞效应测量、氢键酰胺质子的识别、二硫键的已知位置以及主链邻位自旋-自旋耦合常数来确定的。蛋白质的多肽链排列成两个不同的结构域。这些结构域的结构在单独的计算中独立确定，然后组合以获得蛋白质的整体视图。由此确定的主干折叠包括先前使用用于核磁共振数据分析的不同技术识别的规则主干结构元件。距离几何计算还提供了有关弯曲和环的构象以及β-片层扭曲的更多细节。
The polypeptide backbone fold in the solution structure of murine epidermal growth factor has been determined by nuclear magnetic resonance spectroscopy and distance geometry calculations. The results are based on nearly complete sequence-specific resonance assignments and on 333 distance and dihedral-angle constraints; these were determined from nuclear Overhauser effect measurements, identification of hydrogen-bonded amide protons, the known locations of disulfide bonds, and backbone vicinal spin-spin coupling constants. The polypeptide chain of the protein is arranged into two distinct domains. The structures of these domains were determined independently in separate calculations and then combined to obtain an overall view of the protein. The backbone fold thus determined includes the regular backbone structure elements that were previously identified using different techniques for the analysis of the nuclear magnetic resonance data. The distance geometry calculations also provided additional details about the conformations of bends and loops and about the twists of the beta-sheets.