Induction of conductance heterogeneity in gramicidin channels.
Induction of conductance heterogeneity in gramicidin channels.
复制标题
短杆菌肽通道中电导异质性的诱导。
DOI:
10.1021/bi00442a007
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发表时间:
1989
期刊:
影响因子:
2.9
通讯作者:
Andersen,OS
中科院分区:
文献类型:
--
作者:
Sawyer,DB;Koeppe2nd,RE;Andersen,OS
Revised Manuscript Received May 4, 1989 abstract: In previous work from our laboratory, 5-10% of thechannels formed by [Val1] gramicidin A have conductances that fall outside the narrow range that conventionally has defined the standard gramicidin channel [eg, see Russell et al.(1986) Biophys. J. 49, 673], Reports from other laboratories, however, show that up to 50% of [Val'Jgramicidin channels have conductances that fall outside the range for standard channels [eg, see Prasad et al.(1986) Biochemistry 25, 456]. This laboratory-to-laboratory variation in the distribution of gramicidin single-channel conductances suggests that the conductance variants are induced by some environmental factor (s)[Busath etal.(1987) Biophys. J. 51, 79]. In order to test whether extrinsic agents can induce such conductance heterogeneity, we examined the effects of nonionic or zwitterionic detergents upon gramicidin channel behavior. In phospholipid bilayers, detergent addition induces many changes in gramicidin channel behavior: all detergents tested increase the channel appearance rate and average duration; most detergents decrease the conductance of the standard channel; and all but one of the detergents increase the conductance heterogeneity. These results show that the conductance heterogeneity can result from environmental perturbations, thus providing a possible explanationfor the laboratory-to-laboratory variation in the heterogeneity of gramicidin channels. In addition, the differential detergenteffects suggest possible mechanismsby which detergents can induce the conformational perturbations that result in gramicidin single-channel conductance variations..^^. n important problem pertaining to understanding mem-brane protein function is how function depends on the mem-brane environment in which a protein resides. This is a difficult problem toaddress in studies on populations of mem-brane proteins that reside within a sometimes rather poorly controlled native lipid environment. Single-channel studies on membrane-spanning channels in planar lipid bilayers, however, allow the functional consequences of lipid environment modulations to be studiedin detail. Single-channel experiments are particularly useful to examine questions pertaining to the possible heterogeneity among membrane proteins, because one by definition studies single molecular