Dalal S, Balasubramanian S, Regan L
Department of Chemistry, Yale University, New Haven, CT 06520, USA.
Fold Des. 1997;2(5):R71-9. doi: 10.1016/s1359-0278(97)00036-9.
Protein architecture involves two main secondary structural classes: alpha helices and beta sheets. Some natural proteins alter their fold in response to changes in solution conditions or as a consequence of mutation. Here, we discuss recent attempts to induce such conformational changes by design: specifically, the motivation and success of efforts to change one protein fold into a different one in response to the 'Paracelsus Challenge'. The results of such efforts may provide a better understanding of the processes that underlie conformational plasticity in proteins.
α螺旋和β折叠片层。一些天然蛋白质会根据溶液条件的变化或突变而改变其折叠状态。在此,我们讨论最近通过设计诱导此类构象变化的尝试:具体而言,响应“帕拉塞尔苏斯挑战”将一种蛋白质折叠转变为另一种折叠的努力的动机和成果。这些努力的结果可能会让我们更好地理解蛋白质构象可塑性背后的过程。