Observations using Phosphorus-31 nuclear magnetic resonance ((31)P-NMR) of structural changes in freeze-thawed hen egg yolk.
Food Chem. 2018 Apr 01;244:169-176
Authors: Wakamatsu H, Handa A, Chiba K
Abstract
Hen egg yolk (EY) has a complicated structure consisting of lipids and proteins, and its structure is deeply related with its functional properties. (31)P-NMR is an efficient technique to non-destructively detect the dynamic behaviour of phospholipids, the main component of bio-membranes. We determined conditions for measuring the (31)P NMR spectra of EY and identified the components. (31)P-NMR was used to detect phosvitin, inorganic phosphate, and lipoprotein as well as structural changes such as granule collapse and freeze-thaw denaturation as signal changes. Freeze-thaw denaturation generated a new denaturation peak. We separated aggregates of LDL from freeze-thawed plasma using centrifugation. TEM and (31)P-NMR observations revealed that the denaturation peak corresponded to LDL aggregates. The (31)P-NMR spectra suggested the formation of multiple forms of LDL aggregates in which the head groups of phospholipid molecules adopt a face-to-face orientation, similar to that observed following the flocculation of lipoproteins or in the lamellar-like structures of phospholipids.
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Biochemistry. 1990 Aug 21;29(33):7547-57
Authors: Caines GH, Schleich T, Morgan CF, Farnsworth PN
The rotational diffusion behavior of phosphorus metabolites present in calf lens cortical and nuclear homogenates was investigated by the NMR technique of...
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Structural determination of biomolecular interfaces by nuclear magnetic resonance of
Abstract Protein interactions are important for understanding many molecular mechanisms underlying cellular processes. So far, interfaces between interacting proteins have been characterized by NMR spectroscopy mostly by using chemical shift perturbations and cross-saturation via intermolecular cross-relaxation. Although powerful, these techniques cannot provide unambiguous estimates of intermolecular distances between interacting proteins. Here, we present an alternative approach, called REDSPRINT (REDduced/Standard PRoton density INTerface identification), to map protein interfaces with...
Observations using Phosphorus-31 nuclear magnetic resonance ((31)P-NMR) of structural changes in freeze-thawed hen egg yolk.
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