Zhang Z, Pascal S M, Cross T A
Department of Chemistry, Florida State University, Tallahassee 32306-3006.
Biochemistry. 1992 Sep 22;31(37):8822-8. doi: 10.1021/bi00152a019.
A conformational transition is described for the polypeptide, gramicidin A, in which a dimer that forms a left-handed intertwined antiparallel helix is converted to a single-stranded amino terminus to amino terminus right-handed helix. The starting structure is determined here by solution NMR methods while reference is made to the well-established folding motif of gramicidin in a lipid bilayer for the ultimate conformation of this transition. Furthermore, an organic solvent system of benzene and ethanol in which gramicidin has a unique conformation is identified. This conformation is shown to be very similar to that derived from X-ray diffraction of crystals prepared from a similar solvent system.
描述了短杆菌肽A多肽的一种构象转变，其中形成左手缠绕反平行螺旋的二聚体转变为从氨基端到氨基端的单链右手螺旋。这里通过溶液核磁共振方法确定起始结构，同时参考脂质双分子层中短杆菌肽已确立的折叠基序来确定该转变的最终构象。此外，还鉴定出一种苯和乙醇的有机溶剂体系，短杆菌肽在其中具有独特的构象。这种构象显示与由类似溶剂体系制备的晶体的X射线衍射所得到的构象非常相似。
