Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-13960
Curr Opin Struct Biol 1998 Oct 01;85:640-8. doi: 10.1016/s0959-440x(98)80157-7.
Show Gene links Show Anatomy links

NMR structural studies of membrane proteins.

Marassi FM , Opella SJ .


???displayArticle.abstract???
The three-dimensional structures of membrane proteins are essential for understanding their functions, interactions and architectures. Their requirement for lipids has hampered structure determination by conventional approaches. With optimized samples, it is possible to apply solution NMR methods to small membrane proteins in micelles; however, lipid bilayers are the definitive environment for membrane proteins and this requires solid-state NMR methods. Newly developed solid-state NMR experiments enable completely resolved spectra to be obtained from uniformly isotopically labeled membrane proteins in phospholipid lipid bilayers. The resulting operational constraints can be used for the determination of the structures of membrane proteins.

???displayArticle.pubmedLink??? 9818270
???displayArticle.pmcLink??? PMC3282058
???displayArticle.link??? Curr Opin Struct Biol
???displayArticle.grants??? [+]


References [+] :
Almeida, fd coat protein structure in membrane environments: structural dynamics of the loop between the hydrophobic trans-membrane helix and the amphipathic in-plane helix. 1997, Pubmed