期刊
PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES
卷 370, 期 1679, 页码 -出版社
ROYAL SOC
DOI: 10.1098/rstb.2015.0026
关键词
membrane protein; protein folding; protein sorting; chaperone; driving forces; outer membrane protein
类别
资金
- NIH [R01 GM079440]
- NSF [MCB1412108]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1412108] Funding Source: National Science Foundation
In vitro folding studies of outer membrane beta-barrels have been invaluable in revealing the lipid effects on folding rates and efficiencies as well as folding free energies. Here, the biophysical results are summarized, and these kinetic and thermodynamic findings are considered in terms of the requirements for folding in the context of the cellular environment. Because the periplasm lacks an external energy source the only driving forces for sorting and folding available within this compartment are binding or folding free energies and their associated rates. These values define functions for periplasmic chaperones and. suggest a biophysical mechanism for the, BAM complex.
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