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1.
Adv Exp Med Biol ; 302: 453-63, 1991.
Article in English | MEDLINE | ID: mdl-1746344

ABSTRACT

This study has shown the importance of relating NMR spectroscopic information on the water in model food structures to the mechanical properties of those structures. Analysis of the NMR relaxation data can be used to examine the distribution of water domain sizes, and this has been related to the mechanical properties of the samples. A novel NMR probe-head has been designed, which allows both the NMR and the mechanical data to be simultaneously measured during compression of the sample. This probe-head allows compressive stress/strain data to be obtained directly from the NMR sample, allowing changes in the distribution of the water to be directly correlated to changes in mechanical properties.


Subject(s)
Food , Water/chemistry , Chemical Phenomena , Chemistry, Physical , Magnetic Resonance Spectroscopy , Physical Phenomena , Physics
2.
Eur J Biochem ; 109(2): 447-56, 1980 Aug.
Article in English | MEDLINE | ID: mdl-6773775

ABSTRACT

Complete assignments are given for the 13C NMR spectra of hyaluronate and chondroitin in deuterium oxide solution at 50.32 MHz. The assignments published earlier for chondroitin 4-sulphate and chondroitin 6-sulphate were largely confirmed but were found to need some revision in detail. Our conclusions for hyaluronate and the chondroitin sulphates were confirmed by off-resonance experiments based on the proton NMR assignments. The spectra for hyaluronate show line narrowing and chemical shift changes from neutral to alkaline solution which are consistent with, and clearer than, the effects reported earlier for the proton spectra. As before no such changes occur for the chondroitin sulphates. The suggested interpretation is in terms of a conformation change for hyaluronate which originates mainly in altered interaction energies across the 1 leads to 3 linkage with the results that motional freedom is enhanced above that of the parent hyaluronate and even above the chondroitin sulphates. This, and the evidence from a temperature effect, suggests that an additional potential energy minimum is made favourable in alkali so that the overall amplitudes of the bond oscillations are increased.


Subject(s)
Chondroitin Sulfates , Chondroitin , Hyaluronic Acid , Carbohydrate Conformation , Chondroitin/analogs & derivatives , Hydrogen-Ion Concentration , Magnetic Resonance Spectroscopy , Models, Molecular , Structure-Activity Relationship
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