<P><B>Summary</B></P><P>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 found...
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https://www.riss.kr/link?id=A107638765
2008
-
SCOPUS,SCIE
학술저널
787-797(11쪽)
0
상세조회0
다운로드다국어 초록 (Multilingual Abstract)
<P><B>Summary</B></P><P>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 found...
<P><B>Summary</B></P><P>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 ϕ,ψ 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 ϕ,ψ torsion angles for transmembrane α helices and are presented with respect to improving biophysical characterizations of integral membrane proteins.</P>