Whey-protein-isolate-based composite hydrogels with encapsulated black carrot (Daucus carota) extract were prepared by heat-induced gelation. The hydrogels were blended with gum tragacanth, pectin and xanthan gum polysaccharides for modulating their properties. ¹H spin-lattice relaxation experiments were performed in a broad frequency range, from 4 kHz to 30 MHz, to obtain insight into the influence of the different polysaccharides and of the presence of black carrot on dynamical properties of...
[NMR paper] Unveiling protein dynamics in solution with field-cycling NMR relaxometry
Unveiling protein dynamics in solution with field-cycling NMR relaxometry
Field-cycling NMR relaxometry is a well-established technique that can give information on molecular structure and dynamics of biological systems. It provides the nuclear relaxation rates as a function of the applied magnetic field, starting from fields as low as ~ 10^(-4) T up to about 1-3 T. The profiles so collected, called nuclear magnetic relaxation dispersion (NMRD) profiles, can be extended to include the relaxation rates at the largest fields achievable with high resolution NMR...
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[NMR paper] Transport-Relevant Protein Conformational Dynamics and Water Dynamics on Multiple Timescales in an Archetypal Proton Channel - Insights from Solid-State NMR.
Transport-Relevant Protein Conformational Dynamics and Water Dynamics on Multiple Timescales in an Archetypal Proton Channel - Insights from Solid-State NMR.
Transport-Relevant Protein Conformational Dynamics and Water Dynamics on Multiple Timescales in an Archetypal Proton Channel - Insights from Solid-State NMR.
J Am Chem Soc. 2018 Jan 05;:
Authors: Mandala V, Gelenter MD, Hong M
Abstract
The influenza M2 protein forms a tetrameric proton channel that conducts protons from the acidic endosome into the virion by shuttling...
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01-06-2018 11:17 AM
Molecular dynamics-based selectivity for Fast-Field-Cycling relaxometry by Overhauser and solid effect dynamic nuclear polarization #DNPNMR
From The DNP-NMR Blog:
Molecular dynamics-based selectivity for Fast-Field-Cycling relaxometry by Overhauser and solid effect dynamic nuclear polarization #DNPNMR
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Neudert, O., C. Mattea, and S. Stapf, Molecular dynamics-based selectivity for Fast-Field-Cycling relaxometry by Overhauser and solid effect dynamic nuclear polarization. J. Magn. Reson., 2017. 276: p. 113-121.
http://www.sciencedirect.com/science/article/pii/S1090780717300204
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05-23-2017 04:44 AM
TD NMR as a method to determine and characterize the water-binding capacity of whey protein microparticles
TD NMR as a method to determine and characterize the water-binding capacity of whey protein microparticles
Publication date: Available online 9 October 2015
Source:Food Hydrocolloids</br>
Author(s): Jorien P.C.M. Peters, Frank J. Vergeldt, Henk Van As, Hannemieke Luyten, Remko M. Boom, Atze Jan van der Goot</br>
Water-binding capacity (WBC) is commonly measured with a centrifugation method in which a sample is hydrated in excess water and the pellet weight after centrifugation defines the WBC. When a dispersion is being analyzed, here containing whey...
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10-10-2015 06:11 AM
[NMR paper] Structure of hen egg-white lysozyme solvated in TFE/water: a molecular dynamics simulation study based on NMR data.
Structure of hen egg-white lysozyme solvated in TFE/water: a molecular dynamics simulation study based on NMR data.
Related Articles Structure of hen egg-white lysozyme solvated in TFE/water: a molecular dynamics simulation study based on NMR data.
J Biomol NMR. 2013 Mar 14;
Authors: Eichenberger AP, van Gunsteren WF, Smith LJ
Abstract
Various experimental studies of hen egg white lysozyme (HEWL) in water and TFE/water clearly indicate structural differences between the native state and TFE state of HEWL, e.g. the helical content of the...
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03-16-2013 03:18 PM
[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...
Water Dynamics in Whey-Protein-Based Composite Hydrogels by Means of NMR Relaxometry
Linear Mode
