Schiksnis R A, Bogusky M J, Tsang P, Opella S J
Biochemistry. 1987 Mar 10;26(5):1373-81. doi: 10.1021/bi00379a025.
The major coat protein of filamentous bacteriophage adopts its membrane-bound conformation in detergent micelles. High-resolution 1H and 15N NMR experiments are used to characterize the structure and dynamics of residues 30-40 in the hydrophobic midsection of Pf1 coat protein in sodium dodecyl sulfate micelles. Uniform and specific-site 15N labels enable the immobile backbone sites to be identified by their 1H/15N heteronuclear nuclear Overhauser effect and allow the assignment of 1H and 15N resonances. About one-third of the amide N-H protons in the protein undergo very slow exchange with solvent deuterons, which is indicative of sites in highly structured environments. The combination of results from 1H/15N heteronuclear correlation, 1H homonuclear correlation, and 1H homonuclear Overhauser effect experiments assigns the resonances to specific residues and demonstrates that residues 30-40 of the coat protein have a helical secondary structure.
丝状噬菌体的主要外壳蛋白在去污剂胶束中呈现其膜结合构象。高分辨率的1H和15N NMR实验用于表征十二烷基硫酸钠胶束中Pf1外壳蛋白疏水中间部分30 - 40位残基的结构和动力学。均匀和特定位点的15N标记使得通过1H/15N异核核Overhauser效应识别固定的主链位点成为可能，并允许对1H和15N共振进行归属。蛋白质中约三分之一的酰胺N - H质子与溶剂氘核发生非常缓慢的交换，这表明这些位点处于高度结构化的环境中。1H/15N异核相关、1H同核相关和1H同核Overhauser效应实验的结果相结合，将共振归属到特定残基，并证明外壳蛋白的30 - 40位残基具有螺旋二级结构。
