Search results for "disulphide bonds"
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Artificial Oral Processing of Extruded Pea Flour Snacks
2021
International audience; The structure of extruded pea flour can affect chewing performances. Our objective was to relate the bolus properties (fragmentation, moisture content and viscosity) of chewed extruded pea snacks to their structure. In order to have control over oral physiological parameters, we opted for an in vitro approach using a chewing simulator, the variables of which were the flow rate of artificial salivary fluid and chewing time. The structure of the extruded pea snacks was characterized by its density and protein solubility in dithioerythritol (DTE), which reflected the amount of protein aggregates cross-linked by disulphide bonds. The particle size distribution and median…
Identification of disulphide bonds in the refolding of bovine pancreatic RNase A
1996
Background: Comprehension of the rules that govern the folding process is still far from satisfactory, though it is nevertheless clear that all the information required to define the folding is encoded in the amino acid sequence. In proteins that contain disulphide bonds, folding is associated with disulphide bond formation. Protein species with different numbers of disulphides tend to accumulate during the process; these species can be trapped in a stable form, by quenching any remaining free SH groups, and then characterized in order to identify the disulphide bonds formed. Results The refolding pathway of reduced and denatured RNase A has been studied using mass spectrometric strategies …