Publication date: Available online 9 October 2015 Source:Food Hydrocolloids
Author(s): Jorien P.C.M. Peters, Frank J. Vergeldt, Henk Van As, Hannemieke Luyten, Remko M. Boom, Atze Jan van der Goot
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 protein microparticles (MPs), the pellet consists of swollen particles and water between the particles. These two water domains in MP pellets were distinguished using time domain nuclear magnetic resonance (TD NMR). This distinction showed that an increase in WBC from 2 to 5.5 g water/g dry matter was mainly due to an increase in water between the MPs. Besides, it was found that TD NMR-measurements could be used to provide accurate values of the amount of water in both water domains in MP pellets. This makes TD NMR therefore a more accurate method to determine the WBC of the whole pellet than weighing the pellet after centrifugation. Graphical abstract
[NMR paper] Use of a combination of the RDC method and NOESY NMR spectroscopy to determine the structure of Alzheimer's amyloid A?10-35 peptide in solution and in SDS micelles.
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Abstract Protein internal motions influence observables of NMR experiments. The effect of internal motions occurring at the sub-nanosecond timescale can be described by NMR order parameters. Here, we report that the use of order parameters derived from Molecular Dynamics (MD) simulations of two holo-structures of Protein Kinase A increase the discrimination power of INPHARMA, an NMR based methodology that selects docked ligand orientations by maximizing the correlation of...
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TD NMR as a method to determine and characterize the water-binding capacity of whey protein microparticles
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