SOLUTION STRUCTURE OF HUMAN CORTICOTROPIN RELEASING-FACTOR BY H-1-NMR AND DISTANCE GEOMETRY WITH RESTRAINED MOLECULAR-DYNAMICS
SOLUTION STRUCTURE OF HUMAN CORTICOTROPIN RELEASING-FACTOR BY H-1-NMR AND DISTANCE GEOMETRY WITH RESTRAINED MOLECULAR-DYNAMICS
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DOI：
10.1093/protein/6.2.149
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发表时间：
1993-02-01
期刊：
影响因子：
--
通讯作者：
DARBON, H
中科院分区：
文献类型：
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作者：
ROMIER, C;BERNASSAU, JM;DARBON, H
采用质子核磁共振（H-1 NMR）技术，在pH 3.8、37℃条件下，在66%三氟乙醇/34% H2O的混合溶剂体系中测定了人促肾上腺皮质激素释放因子（hCRF）的结构。采用标准二维方法实现了几乎完全的共振分配。通过定性分析残核内部和残核间的超压效应，得到了结构计算的距离约束。通过距离几何获得了距离约束的结构，然后使用分子动力学进行了细化，并使用酰胺氢交换数据完成了结构。在该溶剂中，hCRF的结构包括一个延伸的n端四肽，在残基6和36之间连接一个定义明确的α -螺旋。α -螺旋的前半部分（残基6-20）显然是两性的。5个羧基末端残基主要是无序的。
The structure of human corticotropin releasing factor (hCRF) has been determined by proton nuclear magnetic resonance (H-1 NMR) in a mixed-solvent system of 66% trifluoroethanol/34% H2O at pH 3.8 and 37-degrees-C. Nearly complete resonance assignment was achieved by using standard two-dimensional methods. Distance restraints for structure calculations were obtained by qualitative analysis of intra- and interresidue nuclear Overhauser effects. Structures were obtained from the distance restraints by distance geometry, followed by refinement using molecular dynamics and were completed with amide hydrogen exchange data. The structure of hCRF in this solvent comprises an extended N-terminal tetrapeptide connected to a well-defined alpha-helix between residues 6 and 36. The first half of the alpha-helix (residues 6-20) is clearly amphipathic. The five carboxy-terminal residues are predominantly disordered.