Evidence for rhodopsin refolding during the decay of Meta II.
Evidence for rhodopsin refolding during the decay of Meta II.
复制标题
Meta II 衰变过程中视紫红质重折叠的证据。
DOI:
10.1016/s0006-3495(87)83341-6
复制
发表时间:
1987
影响因子:
3.4
通讯作者:
DeGrip,WJ
中科院分区:
文献类型:
--
作者:
Rothschild,KJ;Gillespie,J;DeGrip,WJ
Fourier transform infrared difference spectroscopy (FTIR) reveals that the Meta II intermediate of the rhodopsin bleaching cascade is structurally distorted relative to rhodopsin. In addition to previously detected alterations in the state of carboxyl groups, a small part of the protein back-bone undergoes a conversion from alpha-helical to beta-type structure. All of these changes partially reverse during Meta II decay. This evidence together with FTIR studies of earlier photointermediates indicates that of the known photointermediates the protein structure of Meta II is the most distorted. It is concluded that light causes rhodopsin to convert into a conformationally distorted form (Meta II), which subsequently refolds into a more rhodopsin-like conformation (opsin).