October 2012
Publication year: 2012 Source:Current Opinion in Structural Biology, Volume 22, Issue 5
Solution NMR spectroscopy can analyze the dynamics of proteins on a wide range of timescales, from picoseconds to even days, in a site-specific manner, and thus its results are complementary to the detailed but largely static structural information obtained by X-ray crystallography. We review recent progresses in a variety of NMR techniques, including relaxation dispersion and paramagnetic relaxation enhancement (PRE), that permit the observation of the low-populated states, which had been ‘invisible’ with other techniques. In addition, we review how NMR spectroscopy can be used to elucidate functionally relevant protein dynamics. Highlights
? Solution NMR can analyze the dynamics of proteins over a wide range of timescales. ? Recent progresses in a variety of NMR techniques are reviewed. ? Relaxation dispersion and PRE are capable of discerning ‘invisible’ low-populated states. ? NMR applications to functionally relevant protein dynamics are also introduced.
Heat Management Strategies for Solid-state NMR of Functional Proteins
Heat Management Strategies for Solid-state NMR of Functional Proteins
Publication year: 2012
Source:Journal of Magnetic Resonance</br>
Daniel J. Fowler, Michael J. Harris, Lynmarie K. Thompson</br>
Modern solid-state NMR methods can acquire high-resolution protein spectra for structure determination. However, these methods use rapid sample spinning and intense decoupling fields that can heat and denature the protein being studied. Here we present a strategy to avoid destroying valuable samples. We advocate first creating a sacrificial sample, which contains unlabeled...
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07-14-2012 01:53 PM
[NMR paper] Solution structure and dynamics of integral membrane proteins by NMR: a case study in
Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP.
Related Articles Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP.
Methods Enzymol. 2005;394:335-50
Authors: Hwang PM, Kay LE
Solution NMR spectroscopy is rapidly becoming an important technique for the study of membrane protein structure and dynamics. NMR experiments on large perdeuterated proteins typically exploit the favorable relaxation properties of backbone amide...
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11-24-2010 11:14 PM
[NMR paper] Differential dynamics in the G protein-coupled receptor rhodopsin revealed by solutio
Differential dynamics in the G protein-coupled receptor rhodopsin revealed by solution NMR.
Related Articles Differential dynamics in the G protein-coupled receptor rhodopsin revealed by solution NMR.
Proc Natl Acad Sci U S A. 2004 Mar 9;101(10):3409-13
Authors: Klein-Seetharaman J, Yanamala NV, Javeed F, Reeves PJ, Getmanova EV, Loewen MC, Schwalbe H, Khorana HG
G protein-coupled receptors are cell-surface seven-helical membrane proteins that undergo conformational changes on activation. The mammalian photoreceptor, rhodopsin, is the...
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11-24-2010 09:25 PM
[NMR paper] Riboflavin synthase of Schizosaccharomyces pombe. Protein dynamics revealed by 19F NM
Riboflavin synthase of Schizosaccharomyces pombe. Protein dynamics revealed by 19F NMR protein perturbation experiments.
Related Articles Riboflavin synthase of Schizosaccharomyces pombe. Protein dynamics revealed by 19F NMR protein perturbation experiments.
BMC Biochem. 2003 Dec 23;4:18
Authors: Fischer M, Schott AK, Kemter K, Feicht R, Richter G, Illarionov B, Eisenreich W, Gerhardt S, Cushman M, Steinbacher S, Huber R, Bacher A
BACKGROUND: Riboflavin synthase catalyzes the transformation of 6,7-dimethyl-8-ribityllumazine into riboflavin in...
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11-24-2010 09:16 PM
[NMR paper] Conformation and backbone dynamics of bacteriorhodopsin revealed by (13)C-NMR.
Conformation and backbone dynamics of bacteriorhodopsin revealed by (13)C-NMR.
Related Articles Conformation and backbone dynamics of bacteriorhodopsin revealed by (13)C-NMR.
Biochim Biophys Acta. 2000 Aug 30;1460(1):39-48
Authors: Saitô H, Tuzi S, Yamaguchi S, Tanio M, Naito A
It is demonstrated here how the secondary structure and dynamics of transmembrane helices, as well as surface residues, such as interhelical loops and N- or C-terminus of bacteriorhodopsin (bR) in purple membrane, can be determined at ambient temperature based on very...
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11-19-2010 08:29 PM
NMR backbone dynamics studies of human PED/PEA-15 outline protein functional sites.
NMR backbone dynamics studies of human PED/PEA-15 outline protein functional sites.
NMR backbone dynamics studies of human PED/PEA-15 outline protein functional sites.
FEBS J. 2010 Sep 3;
Authors: Farina B, Pirone L, Russo L, Viparelli F, Doti N, Pedone C, Pedone EM, Fattorusso R
PED/PEA-15 (phosphoprotein enriched in diabetes/phosphoprotein enriched in astrocytes) is a ubiquitously expressed protein and a key regulator of cell growth and glucose metabolism. PED/PEA-15 mediates both homotypic and heterotypic interactions and is constituted by...
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09-10-2010 11:53 PM
[NMR paper] Phospholipid headgroup dynamics in DOPG-d5-cytochrome c complexes as revealed by 2H a
Phospholipid headgroup dynamics in DOPG-d5-cytochrome c complexes as revealed by 2H and 31P NMR: the effects of a peripheral protein on collective lipid fluctuations.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Phospholipid headgroup dynamics in DOPG-d5-cytochrome c complexes as revealed by 2H and 31P NMR: the effects of a peripheral protein on collective lipid fluctuations.
Solid State Nucl Magn Reson. 1997 Mar;8(1):55-64
Authors: Pinheiro TJ, Duer MJ, Watts A
The...
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08-22-2010 03:31 PM
[NMR paper] Phospholipid headgroup dynamics in DOPG-d5-cytochrome c complexes as revealed by 2H a
Phospholipid headgroup dynamics in DOPG-d5-cytochrome c complexes as revealed by 2H and 31P NMR: the effects of a peripheral protein on collective lipid fluctuations.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Phospholipid headgroup dynamics in DOPG-d5-cytochrome c complexes as revealed by 2H and 31P NMR: the effects of a peripheral protein on collective lipid fluctuations.
Solid State Nucl Magn Reson. 1997 Mar;8(1):55-64
Authors: Pinheiro TJ, Duer MJ, Watts A
The...
Functional dynamics of proteins revealed by solution NMR
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