Transmuting alpha helices and beta sheets

被引:40
作者
Dalal, S
Balasubramanian, S
Regan, L
机构
[1] YALE UNIV, DEPT BIOCHEM & MOL BIOPHYS, NEW HAVEN, CT 06520 USA
[2] YALE UNIV, DEPT CHEM, NEW HAVEN, CT 06520 USA
来源
FOLDING & DESIGN | 1997年 / 2卷 / 05期
关键词
D O I
10.1016/S1359-0278(97)00036-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:R71 / R79
页数:9
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