Department of Structural Biology, University of Pittsburgh School of Medicine, 1051 Biomedical Science Tower 3, 3501 Fifth Avenue, Pittsburgh, Pennsylvania 15261, USA.
J Am Chem Soc. 2012 Mar 7;134(9):4229-35. doi: 10.1021/ja210118w. Epub 2012 Feb 22.
Domain swapping creates protein oligomers by exchange of structural units between identical monomers. At present, no unifying molecular mechanism of domain swapping has emerged. Here we used the protein Cyanovirin-N (CV-N) and (19)F-NMR to investigate the process of domain swapping. CV-N is an HIV inactivating protein that can exist as a monomer or a domain-swapped dimer. We measured thermodynamic and kinetic parameters of the conversion process and determined the size of the energy barrier between the two species. The barrier is very large and of similar magnitude to that for equilibrium unfolding of the protein. Therefore, for CV-N, overall unfolding of the polypeptide is required for domain swapping.
结构域交换通过相同单体之间的结构单元交换形成蛋白质寡聚体。目前,尚未出现结构域交换的统一分子机制。在这里,我们使用蛋白质 Cyanovirin-N(CV-N)和(19)F-NMR 来研究结构域交换的过程。CV-N 是一种 HIV 失活蛋白,可作为单体或结构域交换二聚体存在。我们测量了转换过程的热力学和动力学参数,并确定了两种物质之间的能量势垒大小。该势垒非常大,与蛋白质平衡展开的势垒大小相当。因此,对于 CV-N,结构域交换需要整个多肽的展开。