The effects of anticalcification treatments and hydration on the molecular dynamics of bovine pericardium collagen as revealed by 13C solid-state NMR.
Magn Reson Chem. 2010 Sep;48(9):704-11
Authors: deAzevedo ER, Ayrosa AM, Faria GC, Cervantes HJ, Huster D, Bonagamba TJ, Pitombo RN, Rabbani SR
This article describes a solid-state NMR (SSNMR) investigation of the influence of hydration and chemical cross-linking on the molecular dynamics of the constituents of the bovine pericardium (BP) tissues and its relation to the mechanical properties of the tissue. Samples of natural phenethylamine-diepoxide (DE)- and glutaraldehyde (GL)-fixed BP were investigated by (13)C cross-polarization SSNMR to probe the dynamics of the collagen, and the results were correlated to the mechanical properties of the tissues, probed by dynamical mechanical analysis. For samples of natural BP, the NMR results show that the higher the hydration level the more pronounced the molecular dynamics of the collagen backbone and sidechains, decreasing the tissue's elastic modulus. In contrast, in DE- and GL-treated samples, the collagen molecules are more rigid, and the hydration seems to be less effective in increasing the collagen molecular dynamics and reducing the mechanical strength of the samples. This is mostly attributed to the presence of cross-links between the collagen plates, which renders the collagen mobility less dependent on the water absorption in chemically treated samples.
Collagen atomic scale molecular disorder in ochronotic cartilage from an alkaptonuria patient, observed by solid state NMR.
Collagen atomic scale molecular disorder in ochronotic cartilage from an alkaptonuria patient, observed by solid state NMR.
Collagen atomic scale molecular disorder in ochronotic cartilage from an alkaptonuria patient, observed by solid state NMR.
J Inherit Metab Dis. 2011 Jul 7;
Authors: Chow WY, Taylor AM, Reid DG, Gallagher JA, Duer MJ
In pilot studies of the usefulness of solid state nuclear magnetic resonance spectroscopy in characterizing chemical and molecular structural effects of alkaptonuria on connective tissue, we have obtained...
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07-08-2011 05:21 PM
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR.
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR.
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR.
J Am Chem Soc. 2011 Mar 14;
Authors: Yang J, Aslimovska L, Glaubitz C
Environmental factors such as temperature, hydration, and lipid bilayer properties are tightly coupled to the dynamics of membrane proteins. So far, site-resolved data visualizing the protein's response to alterations in these factors are rare, and conclusions had to be drawn from dynamic data averaged over the whole protein...
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03-16-2011 04:15 PM
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR
Jun Yang, Lubica Aslimovska and Clemens Glaubitz
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja109766n/aop/images/medium/ja-2010-09766n_0011.gif
Journal of the American Chemical Society
DOI: 10.1021/ja109766n
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/VmNlca5pCIw
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03-15-2011 05:56 AM
Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Biophys J. 2010 Nov 17;99(10):3282-9
Authors: Toraya S, Javkhlantugs N, Mishima D, Nishimura K, Ueda K, Naito A
Bombolitin II (BLT2) is one of the hemolytic heptadecapeptides originally isolated from the venom of a bumblebee. Structure and orientation of BLT2 bound to...
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03-03-2011 12:34 PM
[NMR paper] The hydration of amides in helices; a comprehensive picture from molecular dynamics,
The hydration of amides in helices; a comprehensive picture from molecular dynamics, IR, and NMR.
Related Articles The hydration of amides in helices; a comprehensive picture from molecular dynamics, IR, and NMR.
Protein Sci. 2003 Mar;12(3):520-31
Authors: Walsh ST, Cheng RP, Wright WW, Alonso DO, Daggett V, Vanderkooi JM, DeGrado WF
We examined the hydration of amides of alpha(3)D, a simple, designed three-helix bundle protein. Molecular dynamics calculations show that the amide carbonyls on the surface of the protein tilt away from the...
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11-24-2010 09:01 PM
[NMR paper] Solid-state NMR and rigid body molecular dynamics to determine domain orientations of
Solid-state NMR and rigid body molecular dynamics to determine domain orientations of monomeric phospholamban.
Related Articles Solid-state NMR and rigid body molecular dynamics to determine domain orientations of monomeric phospholamban.
J Am Chem Soc. 2002 Aug 14;124(32):9392-3
Authors: Mascioni A, Karim C, Zamoon J, Thomas DD, Veglia G
Solid-state NMR spectroscopy, in conjunction with rigid body molecular dynamics calculations, shows that monomeric phospholamban in lipid bilayers has two distinct helical domains, with an interhelical angle...
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11-24-2010 08:58 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.
Related Articles Solid-state (13)C NMR reveals effects of temperature and hydration on elastin.
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
[NMR paper] NMR and molecular dynamics studies of the hydration of a zinc finger-DNA complex.
NMR and molecular dynamics studies of the hydration of a zinc finger-DNA complex.
Related Articles NMR and molecular dynamics studies of the hydration of a zinc finger-DNA complex.
J Mol Biol. 2000 Oct 6;302(5):1101-17
Authors: Tsui V, Radhakrishnan I, Wright PE, Case DA
The hydration of a high-affinity protein-DNA complex involving the three amino terminal zinc finger domains of transcription factor IIIA (TFIIIA) and a 15-base-pair DNA duplex was investigated by NMR spectroscopy and molecular dynamics (MD) simulations. Intermolecular nuclear...