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利用NMR和分子动力学方法研究了寡肽Asterin B和C的溶液构象.结果表明,Asterin B在溶液中形成了某种非氢键的转角结构,并由残基间的疏水相互作用使整个分子具有两亲性,这种结构特征可能和其生物活性有关.并进一步讨论了这种结构的形成在蛋白质卷曲的起始过程中的意义.而Asterin C在溶液中柔性较大,存在多种构象的平均.
NMR and molecular dynamics methods were used to study the solution conformation of oligopeptides Asterin B and C. The results showed that Asterin B formed some kind of non-hydrogen bond corner structure in solution, and the hydrophobic interaction between the residues made the entire molecule Which may be related to its biological activity, and further discusses the significance of the formation of this structure in the initial process of protein curl.Asterin C is more flexible in solution and has many conformations Average.