van de Ven F J, van Os J W, Aelen J M, Wymenga S S, Remerowski M L, Konings R N, Hilbers C W
Laboratory of Biophysical Chemistry, NSR Center, University of Nijmegen, The Netherlands.
Biochemistry. 1993 Aug 17;32(32):8322-8. doi: 10.1021/bi00083a036.
The major coat protein (gVIIIp) of bacteriophage M13 complexed with SDS detergent micelles was used as a model system to study the lipid-bound conformation of the protein. Conditions were found that allowed the recording of good quality of NMR spectra. By making extensive use of three-dimensional heteronuclear (13C, 15N) NMR, we obtained a complete set of resonance assignments for 1HN, 1H alpha, 1H beta, 13C alpha, CO, and 15N and partially assigned the rest of the 1H spectrum. Analysis of NOE and chemical shift data reveals that gVIIIp is composed of two alpha-helical domains, one ranging from Pro-6 to Glu20 and the other ranging from Tyr-24 all the way to the C-terminus Ser-50. In contrast to the results reported by Henry and Sykes [Henry, G.D., & Sykes, B.D. (1992) Biochemistry 31, 5285-5297], at a high SDS to protein ratio the protein appears to be monomeric.
噬菌体M13的主要外壳蛋白（gVIIIp）与SDS去污剂胶束复合，被用作研究该蛋白脂质结合构象的模型系统。发现了能够记录高质量NMR谱的条件。通过广泛使用三维异核（13C，15N）NMR，我们获得了1HN、1Hα、1Hβ、13Cα、CO和15N的完整共振归属，并对1H谱的其余部分进行了部分归属。对NOE和化学位移数据的分析表明，gVIIIp由两个α-螺旋结构域组成，一个从Pro-6延伸到Glu20，另一个从Tyr-24一直延伸到C端的Ser-50。与Henry和Sykes报道的结果[Henry, G.D., & Sykes, B.D. (1992) Biochemistry 31, 5285-5297]相反，在高SDS与蛋白比例下，该蛋白似乎是单体的。
