Results 41 to 50 of about 414,168 (349)
Calcium Binding and Disulfide Bonds Regulate the Stability of Secretagogin towards Thermal and Urea Denaturation. [PDF]
PLoS ONE, 2016 Secretagogin is a calcium-sensor protein with six EF-hands. It is widely expressed in neurons and neuro-endocrine cells of a broad range of vertebrates including mammals, fishes and amphibia.
Kalyani Sanagavarapu +4 more
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The electrophoresis of transferrins in urea/polyacrylamide gels [PDF]
, 1980 The denaturation of transferrin by urea has been studied by (a) electrophoresis in polyacrylamide gels incorporating a urea gradient, (b) measurements of the loss in iron-binding capacity and (c) u.v. difference spectrometry. In human serum transferrin
Evans, RW, Williams, J
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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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Frontiers in Nutrition, 2022 Marination is a common technology in meat processing with advantages of enhancing tenderness, water retention, and overall quality. This study was conducted to investigate the effect of vacuum tumbling and immersion marination on meat quality ...
Qingfeng Ge +9 more
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Studies on the denaturation of antibody: II. The effect of protein concentration on the rate of denaturation of diphtheria antitoxin by urea [PDF]
, 1945 The specific rate of inactivation of antitoxin in urea solutions, as measured by the Römer neutralization test with toxin, has been shown to be independent of the concentration of protein under the conditions studied.
Wright, George G.
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A calorimetric study of pH-dependent thermal unfolding of leghemoglobin a from soybean [PDF]
, 1998 The purpose of the present work is to study the pH-dependent thermal denaturation of soybean leghemoglobin fraction a in a cyanide complex (Lba.CN) and to compare the results with those of myoglobin (Mb), apomyoglobin (apoMb) and cyanometmyoglobin (Mb.CN)
Mishonova-Alexova, Ekaterina I +1 more
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Identification of key effects causing weak performance of allergen analysis in processed food matrices [PDF]
, 2016 The weaker performance of generally used analytical methods for allergen analysis in processed foods can be connected to protein denaturation. To understand the nature of protein denaturation processes, experimental but realistic model matrices (corn ...
Bugyi, Zs. +5 more
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Journal 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.
Clarkson, JR, Cui, Z, Darton, R
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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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The effect of denaturants on protein structure [PDF]
Protein Science, 1997 AbstractVirtually all studies of the protein‐folding reaction add either heat, acid, or a chemical denaturant to an aqueous protein solution in order to perturb the protein structure. When chemical denaturants are used, very high concentrations are usually necessary to observe any change in protein structure.
Soojay Banerjee +4 more
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