Munson M, O'Brien R, Sturtevant J M, Regan L
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8114.
Protein Sci. 1994 Nov;3(11):2015-22. doi: 10.1002/pro.5560031114.
Rationally redesigned variants of the 4-helix-bundle protein Rop are described. The novel proteins have simplified, repacked, hydrophobic cores and yet reproduce the structure and native-like physical properties of the wild-type protein. The repacked proteins have been characterized thermodynamically and their equilibrium and kinetic thermal and chemical unfolding properties are compared with those of wild-type Rop. The equilibrium stability of the repacked proteins to thermal denaturation is enhanced relative to that of the wild-type protein. The rate of chemically induced folding and unfolding of wild-type Rop is extremely slow when compared with other small proteins. Interestingly, although the repacked proteins are more thermally stable than the wild type, their rates of chemically induced folding and unfolding are greatly increased in comparison to wild type. Perhaps as a consequence of this, their equilibrium stabilities to chemical denaturants are slightly reduced in comparison to the wild type.
本文描述了4-螺旋束蛋白Rop经合理重新设计的变体。这些新型蛋白质具有简化、重新包装的疏水核心，并且能够重现野生型蛋白质的结构和类似天然的物理性质。对重新包装的蛋白质进行了热力学表征，并将其平衡态和动力学热变性及化学变性性质与野生型Rop的性质进行了比较。与野生型蛋白质相比，重新包装的蛋白质对热变性的平衡稳定性有所增强。与其他小蛋白相比，野生型Rop的化学诱导折叠和去折叠速率极其缓慢。有趣的是，尽管重新包装的蛋白质比野生型更耐热，但与野生型相比，它们的化学诱导折叠和去折叠速率大大提高。也许正因如此，与野生型相比，它们对化学变性剂的平衡稳定性略有降低。
