Related ArticlesNature 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 relaxation rate. In this system exchange between water protons and labile protein protons does not dominate the behaviour with temperature of the water-lysozyme intermolecular contribution to the spin-lattice relaxation.
NMR Detection of pH-Dependent Histidine–Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel
NMR Detection of pH-Dependent Histidine–Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel
Fanghao Hu, Klaus Schmidt-Rohr and Mei Hong
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2081185/aop/images/medium/ja-2011-081185_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2081185
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/C3pPoB5_PR8
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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...
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[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...
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[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...
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[NMR paper] NMR relaxation data of water proton in normal tissues.
NMR relaxation data of water proton in normal tissues.
Related Articles NMR relaxation data of water proton in normal tissues.
Physiol Chem Phys Med NMR. 1996;28(4):205-38
Authors: Akber SF
The spin lattice relaxation time (T1) and spin spin relaxation time (T2) of water protons of normal human and animal tissues are archived to up-date those already published. The mechanisms for water proton relaxation times of tissues are reviewed with reference to water content, paramagnetic ion, protein dynamics content and organ weight.
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[NMR paper] NMR study of collagen-water interactions.
NMR study of collagen-water interactions.
Related Articles NMR study of collagen-water interactions.
Biopolymers. 1994 Dec;34(12):1615-26
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...
Nature of lysozyme-water interactions by proton NMR.
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