Journal
STRUCTURE
Volume 16, Issue 5, Pages 787-797Publisher
CELL PRESS
DOI: 10.1016/j.str.2008.02.018
Keywords
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Funding
- NIAID NIH HHS [R01 AI23007, R01 AI023007-21, R01 AI023007-20, R01 AI073891, R01 AI023007-22, R01 AI023007] Funding Source: Medline
- NIGMS NIH HHS [P01 GM064676-04, P01 GM64676, P01 GM064676-05, P01 GM064676] Funding Source: Medline
- National Research Foundation of Korea [과06A1209] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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The environment and unique balance of molecular forces within lipid bilayers has a profound impact upon the structure, dynamics, and function of membrane proteins. We describe the biophysical foundations for the remarkable uniformity of many transmembrane helices that result from the molecular interactions within lipid bilayers. In fact, the characteristic uniformity of transmembrane helices leads to unique spectroscopic opportunities allowing for phi,psi torsion angles to be mapped directly onto solid state nuclear magnetic resonance (NMR) PISEMA spectra. Results from spectral simulations, the solid state NMR-derived structure of the influenza A M2 proton channel transmembrane domain, and high-resolution crystal structures of 27 integral membrane proteins demonstrate that transmembrane helices tend to be more uniform than previously thought. The results are discussed through the definition of a preferred range of backbone 0,4; torsion angles for transmembrane a helices and are presented with respect to improving biophysical characterizations of integral membrane proteins.
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