Publication date: Available online 25 April 2015 Source:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
Author(s): Dominik Demuth , Nils Haase , Daniel Malzacher , Michael Vogel
We use 13C CP MAS NMR to investigate the dependence of elastin dynamics on the concentration and composition of the solvent at various temperatures. For elastin in pure glycerol, line-shape analysis shows that larger-scale fluctuations of the protein backbone require a minimum glycerol concentration of ~0.6 g/g at ambient temperature, while smaller-scale fluctuations are activated at lower solvation levels of ~.2 g/g. Immersing elastin in various glycerol-water mixtures, we observe at room temperature that the protein mobility is higher for lower glycerol fractions in the solvent and, thus, lower solvent viscosity. When decreasing the temperature, the elastin spectra approach the line shape for the rigid protein at 245 K for all studied samples, indicating that the protein ceases to be mobile on the experimental time scale of ~10-5 s. Our findings yield evidence for a strong coupling between elastin fluctuations and solvent dynamics and, hence, such interaction is not restricted to the case of protein-water mixtures. Spectral resolution of different carbon species reveals that the protein-solvent couplings can, however, be different for side chain and backbone units. We discuss these results against the background of the slaving model for protein dynamics.
[NMR paper] Structural studies of adipokinetic hormones in water and DPC micelle solution using NMR distance restrained molecular dynamics.
Structural studies of adipokinetic hormones in water and DPC micelle solution using NMR distance restrained molecular dynamics.
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Peptides. 2014 Mar;53:270-7
Authors: Jackson GE, Gamieldien R, Mugumbate G, Gäde G
Abstract
Melme-CC (pGlu-Leu-Asn-Tyr-Ser-Pro-Asp-Trp...
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[NMR paper] Inverse Temperature Transition of Elastin Like Motifs in Major Ampullate Dragline Silk: MD Simulations of Short Peptides and NMR Studies of Water Dynamics.
Inverse Temperature Transition of Elastin Like Motifs in Major Ampullate Dragline Silk: MD Simulations of Short Peptides and NMR Studies of Water Dynamics.
Related Articles Inverse Temperature Transition of Elastin Like Motifs in Major Ampullate Dragline Silk: MD Simulations of Short Peptides and NMR Studies of Water Dynamics.
Soft Matter. 2014 Feb 7;10(5):773-785
Authors: Ukpebor OT, Shah A, Bazov E, Boutis GS
Abstract
Using deuterium 2D T1-T2 Inverse Laplace Transform (ILT) NMR we have investigated the distribution, population, and...
Glycerol and Glycerol Carbonate as ultraviscous solvents for mixture analysis by NMR
Glycerol and Glycerol Carbonate as ultraviscous solvents for mixture analysis by NMR
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 1 July 2011</br>
Pedro, Lameiras , Leslie, Boudesocque , Zéphirin, Mouloungui , Jean-Hugues, Renault , Jean-Michel, Wieruszeski , ...</br>
NMR of weakly polar analytes in an apolar ultraviscous solvent has recently been proposed for mixture analysis as a pertinent alternative to the DOSY experiment. The present article reports the first use of glycerol and glycerol carbonate as polar...
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07-03-2011 05:40 AM
ESR and NMR studies provide evidence that phosphatidyl glycerol specifically interacts with poxvirus membranes.
ESR and NMR studies provide evidence that phosphatidyl glycerol specifically interacts with poxvirus membranes.
ESR and NMR studies provide evidence that phosphatidyl glycerol specifically interacts with poxvirus membranes.
Virol J. 2010 Dec 31;7(1):379
Authors: Debouzy JC, Crouzier D, Favier AL, Perino J
ABSTRACT: BACKGROUND: The lung would be the first organ targeted in case of the use of Variola virus (the causative agent of smallpox) as a bioweapon. Pulmonary surfactant composed of lipids (90%) and proteins (10%) is considered the major...
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01-05-2011 09:51 PM
[NMR paper] Solid-state (13)C NMR reveals effects of temperature and hydration on elastin.
Solid-state (13)C NMR reveals effects of temperature and hydration on elastin.
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Biophys J. 2002 Feb;82(2):1086-95
Authors: Perry A, Stypa MP, Tenn BK, Kumashiro KK
Elastin is the principal protein component of the elastic fiber in vertebrate tissue. The waters of hydration in the elastic fiber are believed to play a critical role in the structure and function of this largely hydrophobic, amorphous protein. (13)C CPMAS NMR spectra are acquired for...
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11-24-2010 08:49 PM
Investigation of the dynamical properties of water in elastin by deuterium Double Qua
Investigation of the dynamical properties of water in elastin by deuterium Double Quantum Filtered NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Investigation of the dynamical properties of water in elastin by deuterium Double Quantum Filtered NMR.
J Magn Reson. 2010 Jul;205(1):86-92
Authors: Sun C, Boutis GS
The anisotropic motion of tightly bound waters of hydration in bovine nuchal ligament elastin has been studied by deuterium Double Quantum Filtered (DQF) NMR....
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[NMR paper] Carbon-13 NMR studies of alpha-elastin.
Carbon-13 NMR studies of alpha-elastin.
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Ups J Med Sci. 1993;98(1):53-63
Authors: Tarnawski R, Kasperczyk J, Drózdz M
NMR investigations of model protein of elastic fibre is presented. Detailed conformation of alpha-elastin polypeptide chain is discussed by comparison with the conformation of synthetic repeat peptides of elastin. Amino acid composition of alpha-elastin obtained from C-13 NMR spectra correlates with the results of sequencing of tropoelastin.
Effects of solvent concentration and composition on protein dynamics: 13C MAS NMR studies of elastin in glycerol-water mixtures
Linear Mode
