PROTEIN-STRUCTURE BY SOLID-STATE NUCLEAR MAGNETIC-RESONANCE - RESIDUES 40 TO 45 OF BACTERIOPHAGE FD COAT PROTEIN
PROTEIN-STRUCTURE BY SOLID-STATE NUCLEAR MAGNETIC-RESONANCE - RESIDUES 40 TO 45 OF BACTERIOPHAGE FD COAT PROTEIN
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DOI：
10.1016/0022-2836(85)90197-4
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发表时间：
1985-01-01
影响因子：
5.6
通讯作者：
OPELLA, SJ
中科院分区：
文献类型：
--
作者：
CROSS, TA;OPELLA, SJ
用核磁共振法描述了丝状噬菌体fd外壳蛋白部分的三维结构。残基40-45处于稍微扭曲的α-螺旋。这种用于确定蛋白质结构的NMR方法依赖于平行于所施加的磁场定向的蛋白质亚基的对称组装中的化学位移和异源偶极耦合的光谱表现。单个肽连接和病毒粒子的丝轴之间的角度构成了结构信息的基本来源。这些角度与描述蛋白质结构的x，y，z坐标直接相关。
The 3-dimensional strcuture of part of the coat protein in the filamentous bacteriophage fd is described by NMR. Residues 40-45 are in a somewhat distorted .alpha.-helix. This NMR approach for determining protein structure relies on the spectral manifestations of chemical shift and heteronuclear dipolar couplings in a symmetrical assembly of protein subunits oriented parallel to the applied magnetic field. The angles between individual peptide linkages and the filament axis of the virion constitute the basic source of structural information. These angles are directly related to x, y, z coordinates for describing the protein structure.