Schmid F X, Frech C, Scholz C, Walter S
Laboratorium für Biochemie, Universität Bayreuth, Germany.
Biol Chem. 1996 Jul-Aug;377(7-8):417-24.
The small single-domain protein ribonuclease T1 (RNase T1) and variants thereof are good substrates for investigating the mechanisms of catalyzed and assisted protein folding. RNase T1 contains two cis prolines and two disulfide bonds, and the kinetic mechanism of its folding is well known. The wild-type form and designed variants that differ in the number prolines and of disulfide bonds were used as substrates to study the catalysis of folding by prolyl isomerases and protein disulfide isomerases. In its unfolded form, a marginally stable variant of RNase T1 binds to the chaperone GroEL and could thus be used to elucidate the kinetic mechanism of GroEL-mediated protein unfolding.
小单结构域蛋白质核糖核酸酶T1（RNase T1）及其变体是研究催化和辅助蛋白质折叠机制的良好底物。RNase T1含有两个顺式脯氨酸和两个二硫键，其折叠的动力学机制已为人熟知。野生型形式以及脯氨酸数量和二硫键数量不同的设计变体被用作底物，以研究脯氨酰异构酶和蛋白质二硫键异构酶对折叠的催化作用。处于未折叠形式时，RNase T1的一个稳定性略低的变体与伴侣蛋白GroEL结合，因此可用于阐明GroEL介导的蛋白质解折叠的动力学机制。
