Results 1 to 10 of about 284,337 (260)

Protective Effect of Bergapten against Human Erythrocyte Hemolysis and Protein Denaturation In Vitro [PDF]

open access: yesInternational Journal of Inflammation, 2021
Bergapten, a furocoumarin found in many medicinal plants, is used for the management of various conditions. The present in vitro study evaluated the ability of bergapten to prevent human erythrocyte hemolysis and protein denaturation.
Douglas Bosco Aidoo   +3 more
doaj   +2 more sources

Mechanisms of Change in Emulsifying Capacity Induced by Protein Denaturation and Aggregation in Quick-Frozen Pork Patties with Different Fat Levels and Freeze–Thaw Cycles [PDF]

open access: yesFoods, 2021
Herein, we discuss changes in the emulsifying properties of myofibrillar protein (MP) because of protein denaturation and aggregation from quick-frozen pork patties with multiple fat levels and freeze–thaw (F–T) cycles.
Nan Pan   +7 more
doaj   +2 more sources

Protein Denaturation in Foam

open access: yesJournal of Colloid and Interface Science, 1999
The aim of this study was to elucidate the mechanism by which protein molecules become denatured in foam. It was found that damage to the protein is mainly due to surface denaturation at the gas-liquid interface. A fraction of the molecules adsorbed do not refold to their native state when they desorb.
Z F Cui
exaly   +7 more sources

Experimental and Modelling Study of the Denaturation of Milk Protein by Heat Treatment

open access: yesFood Science of Animal Resources, 2017
Heat treatment of milk aims to inhibit the growth of microbes, extend the shelf-life of products and improve the quality of the products. Heat treatment also leads to denaturation of whey protein and the formation of whey protein-casein polymer, which ...
Fang Qian   +5 more
doaj   +2 more sources

Comparison of Characterization Methods for Denaturation Degree of Shrimp Head Protein during Heating

open access: yesShipin gongye ke-ji, 2022
In order to select the suitable characterization method for the denaturation degree of shrimp head protein, the mixed protein extracted from shrimp head was heated at 100 ℃ for a certain time.
Qiumei LIU   +9 more
doaj   +1 more source

Protein stability [determination] problems

open access: yesFrontiers in Molecular Biosciences, 2022
Human health depends on the correct folding of proteins, for misfolding and aggregation lead to diseases. An unfolded (denatured) protein can refold to its original folded state. How does this occur is known as the protein folding problem. One of several
Faizan Ahmad
doaj   +1 more source

Irreversible denaturation of maltodextrin glucosidase studied by differential scanning calorimetry, circular dichroism, and turbidity measurements. [PDF]

open access: yesPLoS ONE, 2014
Thermal denaturation of Escherichia coli maltodextrin glucosidase was studied by differential scanning calorimetry, circular dichroism (230 nm), and UV-absorption measurements (340 nm), which were respectively used to monitor heat absorption ...
Megha Goyal   +2 more
doaj   +1 more source

Highly anomalous energetics of protein cold denaturation linked to folding-unfolding kinetics. [PDF]

open access: yesPLoS ONE, 2011
Despite several careful experimental analyses, it is not yet clear whether protein cold-denaturation is just a "mirror image" of heat denaturation or whether it shows unique structural and energetic features. Here we report that, for a well-characterized
M Luisa Romero-Romero   +3 more
doaj   +1 more source

Modalities of Protein Denaturation and Nature of Denaturants

open access: yesInternational Journal of Pharmaceutical Sciences Review and Research, 2021
Denaturation of protein is a biological phenomenon in which a protein loses its native shape due to the breaking or disruption of weak chemical bonds and interactions which makes the protein biologically inactive. It is the process where properly folded proteins formed under physiological conditions is transformed to an unfolded protein under non ...
Vaishali V. Acharya, Pratima Chaudhuri
openaire   +1 more source

Cold and Warm Denaturation of Proteins [PDF]

open access: yesJournal of Biological Physics, 2001
We introduce a simplified protein model where the water degrees of freedom appear explicitly (although in an extremely simplified fashion). Using this model we are able to recover both the warm and the cold protein denaturation within a single framework, while addressing important issues about the structure of model proteins.
Caldarelli, G., Rios, P. De De
openaire   +5 more sources

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