刊名:Biochimica et Biophysica Acta (BBA) - General Subjects
出版年:2017
出版时间:January 2017
年:2017
卷:1861
期:1
页码:3300-3310
全文大小:1368 K
卷排序:1861
文摘
Bacteriophage T4 homotrimeric sliding clamp gp45 is stable only as a trimer. Perturbing interface interaction causes lowering of thermal & chemical stabilities. gp45 adopts ‘molten globule’-like intermediate state during chemical unfolding. N-ter and C-ter domains affect each other's topology by an inter-domain crosstalk. Interactions with CTD scaffold are necessary for gp45 trimerization and NTD folding.