Results 41 to 50 of about 5,918,106 (339)
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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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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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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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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Journal of Biomolecular NMR, 2001 Chemical shift assignment is reported for the protein ubiquitin denatured in 8M urea at pH 2. The variations in 15N chemical shifts of three different proteins (ubiquitin, disulfide reduced, carboxymethylated lysozyme, all-Ala-alpha-lactalbumin), all without disulfides and denatured in 8M urea at pH 2 are compared to 'random coil shifts' of small model
Peti, W +3 more
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Current Research in Food Science, 2022 Microwave drying (MD) or freeze drying (FD) was commonly used as a drying treatment prior to the extraction of edible insect proteins. However, some quality defects (e.g., lipid oxidation or protein denaturation) were probably occurred via the drying ...
Fengxue Zhang +6 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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, 2018 Traditional (low temperature, long time) and novel (low temperature, short time) sous-vide cooking of lean tuna were characterized by analyzing the effects of thermal protein denaturation (TPD) on quality attributes, such as color, appearance, shrinkage,
Yvan Llave +5 more
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Journal of Chemical Physics, 2018 Complex coacervation can be used as a route to compartmentalize a variety of solutes such as organic small molecules, inorganic nanoparticles, and proteins within microscale coacervate droplets.
Mengmeng Zhao, N. Zacharia
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Fluorescence characterization of denatured proteins [PDF]
Current Opinion in Structural Biology, 2008 Characterization of unfolded states, while critical to a complete understanding of protein folding, is inherently difficult due to structural heterogeneity and dynamic interchange between states. The growing body of work focusing on single molecule fluorescence techniques for the study of protein folding, also highlights their potential for studies of ...
Huimin, Chen, Elizabeth, Rhoades
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