Related ArticlesTechniques and applications of NMR to membrane proteins.
Mol Membr Biol. 2004 May-Jun;21(3):129-41
Authors: Nielsen N, Malmendal A, Vosegaard T
The fact that membrane proteins are notoriously difficult to analyse using standard protocols for atomic-resolution structure determination methods have motivated adaptation of these techniques to membrane protein studies as well as development of new technologies. With this motivation, liquid-state nuclear magnetic resonance (NMR) has recently been used with success for studies of peptides and membrane proteins in detergent micelles, and solid-state NMR has undergone a tremendous evolution towards characterization of membrane proteins in native membrane and oriented phospholipid bilayers. In this mini-review, we describe some of the technological challenges behind these efforts and provide examples on their use in membrane biology.
Protein NMR Spectroscopy: Practical Techniques and Applications - spectroscopyNOW.com
Protein NMR Spectroscopy: Practical Techniques and Applications - spectroscopyNOW.com
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Protein NMR Spectroscopy: Practical Techniques and Applications
spectroscopyNOW.com
Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful technique in structural biology for obtaining high resolution 3-D structures of proteins, second only, and complementary to X-ray crystallography. Molecules are studied in solution, ...
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Postdoc Membrane Proteins
Postdoc Membrane Proteins
Structural studies of membrane proteins by NMR
A post-doctoral position is available to work on the structural studies of a variety of
membrane proteins (cytochrome P450, cytochrome b5, cytochrome-P450-reductase,
and a combination of these proteins to probe protein-protein interactions)
and amyloid proteins using NMR spectroscopy. We are presently utilizing a combination
of high-resolution solution NMR and solid-state (static and MAS) NMR techniques to
solve high-resolution structures and characterize the dynamics of membrane proteins
embedded in suitable...
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01-12-2011 01:45 PM
Recent advances in segmental isotope labeling of proteins: NMR applications to large proteins and glycoproteins
Recent advances in segmental isotope labeling of proteins: NMR applications to large proteins and glycoproteins
Abstract In the last 15 years substantial advances have been made to place isotope labels in native and glycosylated proteins for NMR studies and structure determination. Key developments include segmental isotope labeling using Native Chemical Ligation, Expressed Protein Ligation and Protein Trans-Splicing. These advances are pushing the size limit of NMR spectroscopy further making larger proteins accessible for this technique. It is just emerging that segmental isotope...
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01-09-2011 12:46 PM
[NMR paper] How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
Related Articles How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
Chembiochem. 2005 Sep;6(9):1693-700
Authors: Lorch M, Faham S, Kaiser C, Weber I, Mason AJ, Bowie JU, Glaubitz C
Several studies have demonstrated that it is viable to use microcrystalline preparations of water-soluble proteins as...
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12-01-2010 06:56 PM
Using NMR to study fast dynamics in proteins: methods and applications.
Using NMR to study fast dynamics in proteins: methods and applications.
Related Articles Using NMR to study fast dynamics in proteins: methods and applications.
Curr Opin Pharmacol. 2010 Oct 6;
Authors: Sapienza PJ, Lee AL
Proteins exist not as singular structures with precise coordinates, but rather as fluctuating bodies that move rapidly through an enormous number of conformational substates. These dynamics have important implications for understanding protein function and for structure-based drug design. NMR spectroscopy is particularly well...