作者: R. Scott Houliston , Chengsong Liu , Laila M. R. Singh , Elizabeth M. Meiering
DOI: 10.1021/BI0115838
关键词: Trefoil 、 Amide hydrogen 、 Urea 、 Reaction rate constant 、 Chemistry 、 Ph dependence 、 Hydrogen–deuterium exchange 、 Inorganic chemistry
摘要: Amide hydrogen/deuterium exchange rates were measured as a function of pH and urea for 37 slowly exchanging amides in the β-trefoil protein hisactophilin. The rank order is generally maintained under different solution conditions, trends dependence are correlated with rates. observed consistent expected behavior via global and/or local unfolding. Analysis terms rate constants structural opening closing reveals wide range parts hisactophilin structure. slowest have Many located trefoil 2, but there also some slow trefoils 1 3. Slow exchangers tend to be near interface between β-barrel β-hairpin triplet portions this single-domain Th...