Related ArticlesDetermination of water self-diffusion coefficient in complex food products by low field 1H PFG-NMR: comparison between the standard spin-echo sequence and the T1-weighted spin-echo sequence.
J Magn Reson. 2003 Dec;165(2):265-75
Authors: Métais A, Mariette F
In 1990, Van Den Enden et al. proposed a method for the determination of water droplet size distributions in emulsions using a pulsed-field-gradient nuclear magnetic resonance (PFG-NMR) T1-weighted stimulated-echo technique. This paper describes both the T1-weighted spin-echo sequence, an improved method based on this earlier work, and, the standard PFG spin-echo sequence. These two methods were compared for water self-diffusion coefficient measurement in the fatty protein concentrate sample used as a 'cheese model.' The transversal and longitudinal relaxation parameters T1 and T2 were determined according to the temperature and investigated for each sample; fat-free protein concentrate sample, pure anhydrous milk fat, and fatty protein concentrate sample. The water self-diffusion in fat-free protein concentrate samples followed a linear behavior. Consequently, the water self-diffusion coefficient could be easily characterized for fat-free protein concentrate samples. However, it seemed more complicated to obtain accurate water self-diffusion in fatty protein concentrate samples since the diffusion-attenuation data were fitted by a bi-exponential function. This paper demonstrates that the implementation of the T1-weighted spin-echo sequence, using the different T1 properties of water and fat phases, allows the accurate determination of water self-diffusion coefficient in a food product. To minimize the contribution of the 1H nuclei in the fat phase on the NMR echo signal, the fat protons were selectively eliminated by an additional 180 degrees pulse. This new method reduces the standard errors of diffusion data obtained with a basic spin-echo technique, by a factor of 10. The effectiveness of the use of the T1-weighted spin-echo sequence to perform accurate water self-diffusion coefficients measurement in fatty products is thus demonstrated.
[NMR paper] NMR relaxation and water self-diffusion studies in whey protein solutions and gels.
NMR relaxation and water self-diffusion studies in whey protein solutions and gels.
Related Articles NMR relaxation and water self-diffusion studies in whey protein solutions and gels.
J Agric Food Chem. 2005 Aug 24;53(17):6784-90
Authors: Colsenet R, Mariette F, Cambert M
The changes in water proton transverse relaxation behavior induced by aggregation of whey proteins are explained in terms of the simple molecular processes of diffusion and chemical exchange. The water self-diffusion coefficient was measured in whey protein solutions and...
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[NMR paper] Quantitative measurement of water diffusion lifetimes at a protein/DNA interface by N
Quantitative measurement of water diffusion lifetimes at a protein/DNA interface by NMR.
Related Articles Quantitative measurement of water diffusion lifetimes at a protein/DNA interface by NMR.
J Biomol NMR. 2001 Jun;20(2):111-26
Authors: Gruschus JM, Ferretti JA
Hydration site lifetimes of slowly diffusing water molecules at the protein/DNA interface of the vnd/NK-2 homeodomain DNA complex were determined using novel three-dimensional NMR techniques. The lifetimes were calculated using the ratios of ROE and NOE cross-relaxation rates between...
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[NMR paper] Structure of the metal-water complex in Ras x GDP studied by high-field EPR spectrosc
Structure of the metal-water complex in Ras x GDP studied by high-field EPR spectroscopy and 31P NMR spectroscopy.
Related Articles Structure of the metal-water complex in Ras x GDP studied by high-field EPR spectroscopy and 31P NMR spectroscopy.
Biochemistry. 2001 Feb 20;40(7):1884-9
Authors: Rohrer M, Prisner TF, Brügmann O, Käss H, Spoerner M, Wittinghofer A, Kalbitzer HR
The small GTPase Ras plays a key role as a molecular switch in the intercellular signal transduction. On Mg(2+) --> Mn(2+) substituted samples, the first ligand sphere of...
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[NMR paper] Determination of the diffusion coefficient of insulin and lysozyme in crosslinked dex
Determination of the diffusion coefficient of insulin and lysozyme in crosslinked dextran hydrogels by pulsed-field-gradient NMR.
Related Articles Determination of the diffusion coefficient of insulin and lysozyme in crosslinked dextran hydrogels by pulsed-field-gradient NMR.
Chem Pharm Bull (Tokyo). 1998 Nov;46(11):1836-9
Authors: Aso Y, Yoshioka S, Kojima S
Crosslinked dextran hydrogels were prepared from glycidyl methacrylate (GMA)-derivatized dextran by gamma-irradiation initiation in the presence of insulin and lysozyme as model protein...
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[NMR paper] Determination of the NMR structure of the complex between U1A protein and its RNA pol
Determination of the NMR structure of the complex between U1A protein and its RNA polyadenylation inhibition element.
Related Articles Determination of the NMR structure of the complex between U1A protein and its RNA polyadenylation inhibition element.
J Biomol NMR. 1998 Jan;11(1):59-84
Authors: Howe PW, Allain FH, Varani G, Neuhaus D
RNA-protein recognition is critical to post-transcriptional regulation of gene expression, yet poorly understood at the molecular level. The relatively slow progress in understanding this important area of...
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[NMR paper] Mapping hydration water molecules in the HIV-1 protease/DMP323 complex in solution by
Mapping hydration water molecules in the HIV-1 protease/DMP323 complex in solution by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Mapping hydration water molecules in the HIV-1 protease/DMP323 complex in solution by NMR spectroscopy.
Biochemistry. 1996 Oct 1;35(39):12694-704
Authors: Wang YX, Freedberg DI, Grzesiek S, Torchia DA, Wingfield PT, Kaufman JD, Stahl SJ, Chang CH, Hodge CN
A tetrahedrally hydrogen-bonded structural water molecule, water 301, is seen in...
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[NMR paper] Determination of the NMR solution structure of a specific DNA complex of the Myb DNA-
Determination of the NMR solution structure of a specific DNA complex of the Myb DNA-binding domain.
Related Articles Determination of the NMR solution structure of a specific DNA complex of the Myb DNA-binding domain.
J Biomol NMR. 1995 Nov;6(3):294-305
Authors: Morikawa S, Ogata K, Sekikawa A, Sarai A, Ishii S, Nishimura Y, Nakamura H
The solution structure of a specific DNA complex of the minimum DNA-binding domain of the mouse c-Myb protein was determined by distance geometry calculations using a set of 1732 nuclear Overhauser enhancement...
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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...