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Experimental and Modelling Study of the Denaturation of Milk Protein by Heat Treatment
Food 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
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Trends in Peptide and Protein Sciences, 2019 The protein molecules experience various external stresses leading to denaturation of protein during the process of transforming original whey to the concentrated whey proteins or while the concentrated proteins are used in the protein-enriched food ...
Md. Amdadul Haque +3 more
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Jurnal Kimia Riset, 2022 Inflammation is a normal protective reaction against tissue damage caused by physical injury, harmful chemicals, and protein denaturation. Protein denaturation is a process in which proteins lose their tertiary structure and secondary structure due to ...
Dwi Fitriyani, Raden Fatahillah
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Microscopic mechanism for cold denaturation [PDF]
, 2007 We elucidate the mechanism of cold denaturation through constant-pressure simulations for a model of hydrophobic molecules in an explicit solvent. We find that the temperature dependence of the hydrophobic effect is the driving force/induces/facilitates ...
Ala-Nissila, Tapio +4 more
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The manufacture of antibodies in vitro [PDF]
, 1942 A protein solution with the properties of a specific antiserum to the triphenylmethane dye methyl blue has been made by treating a solution of bovine gamma-globulin and the dye with alkali and then slowly neutralizing the alkali.
Campbell, Dan H., Pauling, Linus
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Immunological Characteristics of Denatured Proteins [PDF]
Nature, 1966 AFTER denaturation, some characteristic changes occur in the properties of proteins, among which are variations in immunological features. For example, the specific immunological behaviour of ovalbumin is altered and its antigenic capacity decreases considerably1–3.
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Determination of Pseudokinase-ligand Interaction by a Fluorescence-based Thermal Shift Assay
Bio-Protocol, 2014 This protocol describes a robust technique for the measurement of pseudokinase-ligand interaction by a fluorescence-based Thermal Shift Assay (TSA).
Isabelle Lucet +7 more
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Polar or apolar--the role of polarity for urea-induced protein denaturation. [PDF]
PLoS Computational Biology, 2008 Urea-induced protein denaturation is widely used to study protein folding and stability; however, the molecular mechanism and driving forces of this process are not yet fully understood.
Martin C Stumpe, Helmut Grubmüller
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The role of a disulfide bridge in the stability and folding kinetics of Arabidopsis thaliana cytochrome c6A [PDF]
, 2011 Cytochrome c 6A is a eukaryotic member of the Class I cytochrome c family possessing a high structural homology with photosynthetic cytochrome c 6 from cyanobacteria, but structurally and functionally distinct through the presence of a disulfide bond and
Arslan +64 more
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Conformational Isomerization Involving Conserved Proline Residues Modulates Oligomerization of the NS1 Interferon Response Inhibitor from the Syncytial Respiratory Virus [PDF]
, 2019 Interferon response suppression by the respiratory syncytial virus relies on two unique nonstructural proteins, NS1 and NS2, that interact with cellular partners through high-order complexes.
Alonso, Leonardo Gabriel +9 more
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