Authors: Renou JP, Bonnet M, Bielicki G, Rochdi A, Gatellier P
A proton magnetic resonance study of different cross-linked collagens was performed as a function of water content and temperature. Collagens from three connective tissues (calf, steer, and cow) were chosen according to the different number of nonreducible multivalent cross-links, which increases during the life of animal. Samples were hydrated under five well-defined water activities (Aw) ranging from 0.44 to 0.85. The transverse and cross-relaxation times of water protons were studied as a function of temperature from -20 up to 100 degrees C. From the temperature dependence of relaxation rates, the dynamics of water molecules can be described according to different processes: exchange of protons at the higher temperatures and dipole-dipole interactions that prevail at the lower temperatures. The exchange processes are analyzed as a function of the residence lifetime of water molecules at the protein interface and of the transfer of spin energy from water protons to macromolecule protons. The proton dipole-dipole interactions are related to the relaxation parameters of protein and water protons. All the relaxation parameters showed specific behavior for the 0.44 water activity for every tissue. The collagen tissue from calf also showed distinct behavior in comparison with other tissues.
Insight into interactions of the von-Willebrand-factor-A-like domain 2 with the FNIII-like domain 9 of collagen VII by NMR and SPR.
Insight into interactions of the von-Willebrand-factor-A-like domain 2 with the FNIII-like domain 9 of collagen VII by NMR and SPR.
Insight into interactions of the von-Willebrand-factor-A-like domain 2 with the FNIII-like domain 9 of collagen VII by NMR and SPR.
FEBS Lett. 2011 May 9;
Authors: Leineweber S, Schönig S, Seeger K
Type VII collagen as component of anchoring fibrils plays an important role in skin architecture, however, no detailed structural information is available. Here, we describe the recombinant expression, isotope labeling, and...
nmrlearner
Journal club
0
05-17-2011 06:21 PM
Site-resolved measurement of water-protein interactions by solution NMR.
Site-resolved measurement of water-protein interactions by solution NMR.
Site-resolved measurement of water-protein interactions by solution NMR.
Nat Struct Mol Biol. 2011 Jan 2;
Authors: Nucci NV, Pometun MS, Wand AJ
The interactions of biological macromolecules with water are fundamental to their structure, dynamics and function. Historically, characterization of the location and residence times of hydration waters of proteins in solution has been quite difficult. Confining proteins within the nanoscale interior of a reverse micelle slows water...
nmrlearner
Journal club
0
01-05-2011 09:51 PM
[NMR paper] Water-protein interactions in microcrystalline crh measured by 1H-13C solid-state NMR
Water-protein interactions in microcrystalline crh measured by 1H-13C solid-state NMR spectroscopy.
Related Articles Water-protein interactions in microcrystalline crh measured by 1H-13C solid-state NMR spectroscopy.
J Am Chem Soc. 2003 Nov 5;125(44):13336-7
Authors: Lesage A, Böckmann A
Using solid-state NMR carbon-proton dipolar correlation spectroscopy, we observed hydrogen exchange on the millisecond time scale between water molecules and protein protons in a solid sample. These interactions are shown to be related to important structural...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] Multiple quantum filtered NMR studies of the interaction between collagen and water i
Multiple quantum filtered NMR studies of the interaction between collagen and water in the tendon.
Related Articles Multiple quantum filtered NMR studies of the interaction between collagen and water in the tendon.
J Am Chem Soc. 2002 Mar 27;124(12):3125-32
Authors: Eliav U, Navon G
We studied the physical processes and the chemical reactions involved in magnetization transfer between water and large proteins, such as collagen, in bovine Achilles tendon. Since the NMR spectrum for such proteins is broadened by very large dipolar interactions,...
nmrlearner
Journal club
0
11-24-2010 08:49 PM
[NMR paper] Effect of thermal denaturation on water-collagen interactions: NMR relaxation and dif
Effect of thermal denaturation on water-collagen interactions: NMR relaxation and differential scanning calorimetry analysis.
Related Articles Effect of thermal denaturation on water-collagen interactions: NMR relaxation and differential scanning calorimetry analysis.
Biopolymers. 1999 Dec;50(7):690-6
Authors: Rochdi A, Foucat L, Renou JP
The dependence of the proton spin-lattice relaxation rate, and of the enthalpy and temperature of denaturation on water content, were studied by nmr and differential scanning calorimetry (DSC) in native and...
nmrlearner
Journal club
0
11-18-2010 08:31 PM
[NMR paper] 31P solid-state NMR measurements used to detect interactions between NADPH and water
31P solid-state NMR measurements used to detect interactions between NADPH and water and to determine the ionisation state of NADPH in a protein-ligand complex subjected to low-level hydration.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 31P solid-state NMR measurements used to detect interactions between NADPH and water and to determine the ionisation state of NADPH in a protein-ligand complex subjected to low-level hydration.
Eur J Biochem. 1996 Jan...
nmrlearner
Journal club
0
08-22-2010 02:27 PM
[NMR paper] Nature of lysozyme-water interactions by proton NMR.
Nature of lysozyme-water interactions by proton NMR.
Related Articles Nature of lysozyme-water interactions by proton NMR.
Biochem Cell Biol. 1991 May-Jun;69(5-6):341-5
Authors: Prosser S, Peemoeller H
Proton spin-lattice relaxation measurements were performed in 10 mM lysozyme solution as a function of temperature and degree of substitution of solvent H2O with D2O. The results show that in the temperature range from 274 to 323 K, the intermolecular lysozyme proton water proton coupling contributes appreciably to the observed water proton...
nmrlearner
Journal club
0
08-21-2010 11:16 PM
[NMR paper] Protein-water interactions from 2H NMR relaxation studies: influence of hydrophilic,
Protein-water interactions from 2H NMR relaxation studies: influence of hydrophilic, hydrophobic, and electrostatic interactions.
Related Articles Protein-water interactions from 2H NMR relaxation studies: influence of hydrophilic, hydrophobic, and electrostatic interactions.
Adv Exp Med Biol. 1991;302:541-60
Authors: Kumosinski TF, Pessen H, Farrell HM
The importance of water interactions with proteins in food systems is well documented. A controversy exists, however, as to the nature of these interactions and the effect of protein structural...
NMR study of collagen-water interactions.
Linear Mode
