期刊
CURRENT PHARMACEUTICAL DESIGN
卷 20, 期 8, 页码 1268-1273出版社
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/13816128113199990071
关键词
beta-barrel membrane proteins; protein-protein interaction; weakly stable regions; VDAC; Tom40; OmpF
资金
- NIH [GM079804]
- NSF [DMS-0800257, DBI-1062328]
- ONR [N00014-09-1-0028]
- Fulbright Fellowship
- Higher Education Commission of Pakistan
- Chinese Academy of Sciences Fellowship for Young International Scientist [2012Y1SB0006]
- China Natural National Science Foundation [31250110524]
We briefly discuss recent progress in computational characterization of the sequence and structural properties of beta-barrel membrane properties. We discuss the emerging concept of weakly stable regions in beta-barrel membrane proteins, computational methods to identify these regions and mechanisms adopted by beta-barrel membrane proteins in nature to stabilize them. We further discuss computational methods to identify protein-protein interactions in beta-barrel membrane proteins and recent experimental studies that aim at altering the biophysical properties including oligomerization state and stability of beta-barrel membrane proteins based on the emerging organization principles of these proteins from recent computational studies.
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