Abstract
The combination of high-resolution NMR spectroscopy with pressure perturbation, known as variable-pressure NMR spectroscopy or simply high pressure NMR spectroscopy, is a relatively recent accomplishment, but is a technique expanding rapidly with high promise in future. The importance of the method is that it allows, for the first time in history, a systematic means of detecting and analyzing the structures and thermodynamic stability of high-energy sub-states in proteins. High-energy sub-states have been only vaguely known so far, as normally their populations are too low to be detected by conventional spectroscopic techniques including NMR spectroscopy. By now, however, high pressure NMR spectroscopy has established unequivocally that high-energy conformers are universally present in proteins in equilibrium with their stable folded counterparts. This chapter describes briefly the techniques of high pressure NMR spectroscopy and its unique and novel aspects as a method to explore protein structure in its high-energy paradigm with illustrative examples. It is now well established that high pressure NMR spectroscopy is a method to study intrinsic fluctuations of proteins, rather than those forced by pressure, by detecting structural changes amplified by pressure. Extension of the method to other bio-macromolecular systems is considered fairly straightforward.
PMID: 26174406 [PubMed - as supplied by publisher]
[NMR paper] Cavity as a Source of Conformational Fluctuation and High-Energy State: High-Pressure NMR Study of a Cavity-Enlarged Mutant of T4Lysozyme.
Cavity as a Source of Conformational Fluctuation and High-Energy State: High-Pressure NMR Study of a Cavity-Enlarged Mutant of T4Lysozyme.
Cavity as a Source of Conformational Fluctuation and High-Energy State: High-Pressure NMR Study of a Cavity-Enlarged Mutant of T4Lysozyme.
Biophys J. 2015 Jan 6;108(1):133-145
Authors: Maeno A, Sindhikara D, Hirata F, Otten R, Dahlquist FW, Yokoyama S, Akasaka K, Mulder FA, Kitahara R
Abstract
Although the structure, function, conformational dynamics, and controlled thermodynamics of proteins...
nmrlearner
Journal club
0
01-08-2015 01:29 PM
[NMR paper] Distinct conformational states of the Alzheimer ?-amyloid peptide can be detected by high-pressure NMR spectroscopy.
Distinct conformational states of the Alzheimer ?-amyloid peptide can be detected by high-pressure NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Distinct conformational states of the Alzheimer ?-amyloid peptide can be detected by high-pressure NMR spectroscopy.
Angew Chem Int Ed Engl. 2013 Aug 19;52(34):8943-7
Authors: Munte CE, Beck Erlach M, Kremer W, Koehler J, Kalbitzer HR
PMID: 23843225
nmrlearner
Journal club
0
06-06-2014 03:59 PM
[NMR paper] Intrinsic Allosteric Inhibition of Signaling Proteins by Targeting Rare Interaction States Detected by High-Pressure NMR Spectroscopy.
Intrinsic Allosteric Inhibition of Signaling Proteins by Targeting Rare Interaction States Detected by High-Pressure NMR Spectroscopy.
Related Articles Intrinsic Allosteric Inhibition of Signaling Proteins by Targeting Rare Interaction States Detected by High-Pressure NMR Spectroscopy.
Angew Chem Int Ed Engl. 2013 Nov 11;
Authors: Kalbitzer HR, Rosnizeck IC, Munte CE, Narayanan SP, Kropf V, Spoerner M
Abstract
A new type of allosteric inhibition by small molecules is proposed that should be applicable to all proteins involved intrinsically...
nmrlearner
Journal club
0
11-13-2013 09:22 PM
[NMR paper] Impact of Hydrostatic Pressure on an Intrinsically Disordered Protein: A High-Pressure NMR Study of ?-Synuclein.
Impact of Hydrostatic Pressure on an Intrinsically Disordered Protein: A High-Pressure NMR Study of ?-Synuclein.
Related Articles Impact of Hydrostatic Pressure on an Intrinsically Disordered Protein: A High-Pressure NMR Study of ?-Synuclein.
Chembiochem. 2013 Jun 28;
Authors: Roche J, Ying J, Maltsev AS, Bax A
Abstract
The impact of pressure on the backbone (15) N, (1) H and (13) C chemical shifts in N-terminally acetylated ?-synuclein has been evaluated over a pressure range 1-2500 bar. Even while the chemical shifts fall very close...
nmrlearner
Journal club
0
07-03-2013 01:46 PM
[Question from NMRWiki Q&A forum] High Pressure NMR Samples
High Pressure NMR Samples
I need to run NMR on samples of anhydrous ammonia. The boiling point of anhydrous ammonia is -33.34 deg C. In order to be able to have enough time to acquire spectra, I would like to seal the NMR tubes. Once the sample tubes are sealed, the ammonia will build up pressure until it reaches equilibrium and exists as a liquid at room temperature (at approximately 10 atm of pressure). I know NMR tubes exist which can easily withstand these sorts of pressures, but my main problem is in finding a way to seal the tube. I have tried sealing the tubes by melting the...
nmrlearner
News from other NMR forums
0
02-23-2012 09:08 PM
High-Pressure in Situ 129Xe NMR Spectroscopy and Computer Simulations of Breathing Transitions in the Metal–Organic Framework Ni2(2,6-ndc)2(dabco) (DUT-8(Ni))
High-Pressure in Situ 129Xe NMR Spectroscopy and Computer Simulations of Breathing Transitions in the Metal–Organic Framework Ni2(2,6-ndc)2(dabco) (DUT-8(Ni))
Herbert C. Hoffmann, Bassem Assfour, Fanny Epperlein, Nicole Klein, Silvia Paasch, Irena Senkovska, Stefan Kaskel, Gotthard Seifert and Eike Brunner
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja201951t/aop/images/medium/ja-2011-01951t_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/ja201951t
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
nmrlearner
Journal club
0
05-16-2011 08:23 PM
[NMR paper] High-pressure NMR spectroscopy for characterizing folding intermediates and denatured
High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins.
Related Articles High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins.
Methods. 2004 Sep;34(1):133-43
Authors: Kamatari YO, Kitahara R, Yamada H, Yokoyama S, Akasaka K
Extensive structural studies using high-pressure NMR spectroscopy have recently been carried out on proteins, which potentially contribute to our understanding of the mechanisms of protein folding. Pressure shifts the...
nmrlearner
Journal club
0
11-24-2010 10:01 PM
[NMR images] High pressure NMR spectroscopy
http://www.biologie.uni-regensburg.de/Biophysik/Kalbitzer/c2c/Grafik/pArnold_1.jpg
biologie.uni-regensburg.de
1/11/2010 8:48:44 AM GMT
High pressure NMR spectroscopy
More...
High Pressure NMR Spectroscopy.
Linear Mode
