Aggregation and assembly of phage P22 temperature-sensitive coat protein mutants in vitro mimic the in vivo phenotype.
Aggregation and assembly of phage P22 temperature-sensitive coat protein mutants in vitro mimic the in vivo phenotype.
复制标题
噬菌体 P22 温度敏感外壳蛋白突变体的体外聚集和组装模拟体内表型。
DOI：
10.1021/bi982739f
复制
发表时间：
1999
期刊：
影响因子：
--
通讯作者：
Teschke,CM
中科院分区：
文献类型：
--
作者：
Teschke,CM
Aggregation is a common side reaction in the folding of proteins which is likely due to inappropriate interactions of folding intermediates. In the in vivo folding of phage P22 coat protein, amino acid substitutions that cause a temperature-sensitive-folding (tsf) phenotype lead to the localization of the mutant coat proteins to inclusion bodies. Investigated here is the aggregation of wild-type (WT) coat protein and 3tsfmutants of coat protein. Thetsfcoat proteins aggregated when refolded in vitro at high temperature. If thetsfcoat proteins were refolded at 4 °C, they were able attain an assembly active state. WT coat protein, on the other hand, did not aggregate significantly even when folded at high temperature. The refoldedtsfmutants exhibited altered secondary and tertiary structures and had an increased surface hydrophobicity, which may explain the increased propensity of their folding intermediates to aggregate.
