Related ArticlesRelaxation of water protons in highly concentrated aqueous protein systems studied by 1H NMR spectroscopy.
Z Naturforsch C. 2001 Nov-Dec;56(11-12):1075-81
Authors: Szuminska K, Gutsze A, Kowalczyk A
Concentrated Aqueous Protein Systems, Proton Relaxation Times, Slow Chemical Exchange In this paper we present proton spin-lattice (T1) and spin-spin (T2) relaxation times measured vs. concentration, temperature, pulse interval (tauCPMG) as well as 1H NMR spectral measurements in a wide range of concentrations of bovine serum albumin (BSA) solutions. The anomalous relaxation behaviour of the water protons, similar to that observed in mammalian lenses, was found in the two most concentrated solutions (44% and 46%). The functional dependence of the spin-spin relaxation time vs. tauCPMG pulse interval and the values of the motional activation parameters obtained from the temperature dependencies of spin-lattice relaxation times suggest that the water molecule mobility is reduced in these systems. The slow exchange process on the T2 time scale is proposed to explain the obtained data. The proton spectral measurements support the hypothesis of a slow exchange mechanism in the highest concentrated solutions. From the analysis of the shape of the proton spectra the mean exchange times between bound and bulk water proton groups (tauex) have been estimated for the range of the highest concentrations (30%-46%). The obtained values are of the order of milliseconds assuring that the slow exchange condition is fulfilled in the most concentrated samples.
Using the water signal to detect invisible exchanging protons in the catalytic triad of a serine protease
Using the water signal to detect invisible exchanging protons in the catalytic triad of a serine protease
Abstract Chemical Exchange Saturation Transfer (CEST) is an MRI approach that can indirectly detect exchange broadened protons that are invisible in traditional NMR spectra. We modified the CEST pulse sequence for use on high-resolution spectrometers and developed a quantitative approach for measuring exchange rates based upon CEST spectra. This new methodology was applied to the rapidly exchanging Hδ1 and Hε2 protons of His57 in the catalytic triad of bovine chymotrypsinogen-A...
[NMR paper] NMR spectroscopic detection of protein protons and longitudinal relaxation rates betw
NMR spectroscopic detection of protein protons and longitudinal relaxation rates between 0.01 and 50 MHz.
Related Articles NMR spectroscopic detection of protein protons and longitudinal relaxation rates between 0.01 and 50 MHz.
Angew Chem Int Ed Engl. 2005 Apr 8;44(15):2223-5
Authors: Bertini I, Gupta YK, Luchinat C, Parigi G, Schlörb C, Schwalbe H
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[NMR paper] 14N NMR relaxation times of several protein amino acids in aqueous solution--comparis
14N NMR relaxation times of several protein amino acids in aqueous solution--comparison with 17O NMR data and estimation of the relative hydration numbers in the cationic and zwitterionic forms.
Related Articles 14N NMR relaxation times of several protein amino acids in aqueous solution--comparison with 17O NMR data and estimation of the relative hydration numbers in the cationic and zwitterionic forms.
J Magn Reson. 2003 Oct;164(2):294-303
Authors: Troganis AN, Tsanaktsidis C, Gerothanassis IP
The 14N nuclear magnetic resonance (NMR)...
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[NMR paper] NMR spectroscopy of hydroxyl protons in aqueous solutions of peptides and proteins.
NMR spectroscopy of hydroxyl protons in aqueous solutions of peptides and proteins.
Related Articles NMR spectroscopy of hydroxyl protons in aqueous solutions of peptides and proteins.
J Biomol NMR. 1992 Sep;2(5):447-65
Authors: Liepinsh E, Otting G, Wüthrich K
Hydroxyl groups of serine and threonine, and to some extent also tyrosine are usually located on or near the surface of proteins. NMR observations of the hydroxyl protons is therefore of interest to support investigations of the protein surface in solution, and knowledge of the...
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[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...
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[NMR paper] Fluctuations, exchange processes, and water diffusion in aqueous protein systems: A s
Fluctuations, exchange processes, and water diffusion in aqueous protein systems: A study of bovine serum albumin by diverse NMR techniques.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Fluctuations, exchange processes, and water diffusion in aqueous protein systems: A study of bovine serum albumin by diverse NMR techniques.
Biophys J. 1990 Nov;58(5):1183-97
Authors: Kimmich R, Gneiting T, Kotitschke K, Schnur G
Experimental frequency, concentration, and...
Relaxation of water protons in highly concentrated aqueous protein systems studied by
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