Optimizing the fold stability of the circularly permuted Trp-cage motif.
Optimizing the fold stability of the circularly permuted Trp-cage motif.
复制标题
优化循环排列的色氨酸笼基序的折叠稳定性。
DOI：
10.1002/bip.23327
复制
发表时间：
2019
期刊：
影响因子：
2.9
通讯作者：
Andersen,NielsH
中科院分区：
文献类型：
--
作者：
Graham,KatherineA;Byrne,Aimee;Mason,Micheal;Andersen,NielsH
通过连接区和关键稳定突变的优化，可以提高循环排列（cp）Trp-笼小蛋白的稳定性。然而，即使是最稳定的色氨酸笼圆形排列仍然不如类似的标准拓扑（std）色氨酸笼稳定。将 Trp 笼折叠稳定性的突变研究扩展到 cp 物种（包括缺乏链末端电荷的类似物），发现并定量了一些额外的稳定和不稳定相互作用。质子化后，圆形排列的不稳定程度比标准拓扑系列大得多。末端效应，特别是库仑相互作用，对于 cp 系列似乎更为重要，而 cp 系列中的 Y10/P4 相互作用并不像标准拓扑系列中相应的 Y3/P19 那样具有重要的稳定特征。
Through optimization of the linker region and key stabilizing mutations, it has been possible to improve the stability of the circularly permuted (cp) Trp‐cage miniprotein. However, even the most stable Trp‐cage circular permutants are still less stable than the analogous standard topology (std) Trp‐cages. Extending mutational studies of Trp‐cage fold stability to cp‐species, including analogs lacking chain terminal charges, has uncovered and quantitated some additional stabilizing and destabilizing interactions. Upon protonation, the circular permutants are destabilized to a much greater extent than the standard topology series. End effects, particularly Coulombic interactions, appear to be more important for the cp‐series while the Y10/P4 interaction in the cp‐series is not as significant a stabilizing feature as the corresponding Y3/P19 in the standard topology series.