期刊
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
卷 42, 期 10, 页码 731-755出版社
SPRINGER
DOI: 10.1007/s00249-013-0925-x
关键词
Membrane proteins; Solid-state NMR; Lipids; Membrane protein crystallography
类别
资金
- NIH [AI 074805, AI 073891, AI 023007]
- National Science Foundation [0654118]
- Medical Research Council (MRC)
- Engineering and Physical Sciences Research Council (EPSRC), UK
- Engineering and Physical Sciences Research Council [EP/E000290/1] Funding Source: researchfish
- EPSRC [EP/E000290/1] Funding Source: UKRI
Evidence that membrane proteins respond conformationally and functionally to their environment is growing. Structural models, by necessity, have been characterized in preparations where the protein has been removed from its native environment. Different structural methods have used various membrane mimetics that have recently included lipid bilayers as a more native-like environment. Structural tools applied to lipid bilayer-embedded integral proteins are informing us about important generic characteristics of how membrane proteins respond to the lipid environment as compared with their response to other nonlipid environments. Here, we review the current status of the field, with specific reference to observations of some well-studied alpha-helical membrane proteins, as a starting point to aid the development of possible generic principles for model refinement.
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