NMR structural studies of membrane proteins. Curr Opin Struct Biol 1998 Oct;8(5):640-8
Date
11/18/1998Pubmed ID
9818270Pubmed Central ID
PMC3282058DOI
10.1016/s0959-440x(98)80157-7Scopus ID
2-s2.0-0031764019 (requires institutional sign-in at Scopus site) 138 CitationsAbstract
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.
Author List
Marassi FM, Opella SJAuthor
Francesca M. Marassi PhD Chair, Professor in the Biophysics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Anti-Bacterial AgentsAntimicrobial Cationic Peptides
Capsid
Lipid Bilayers
Magnetic Resonance Spectroscopy
Membrane Proteins
Peptides
Protein Conformation
Receptors, Cholinergic
Xenopus Proteins
