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Critical reviews in food science and nutrition, 2022
Frozen storage is most widely adopted preservation method to maintain food freshness and nutritional attributes. However, at low temperature, food is prone to chemical changes such as protein denaturation and lipid oxidation. In this review, we discussed
Gaopeng Zhang +5 more
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Frozen storage is most widely adopted preservation method to maintain food freshness and nutritional attributes. However, at low temperature, food is prone to chemical changes such as protein denaturation and lipid oxidation. In this review, we discussed
Gaopeng Zhang +5 more
semanticscholar +1 more source
Annual Review of Biochemistry, 1991
The denatured "state" of a protein is a distribution of many different molecular conformations, the averages of which are measured by experiments. The properties of this ensemble depend sensitively on the solution conditions. There is now considerable evidence that even in strong denaturants such as 6M GuHC1 and 9M urea, some structure may remain in ...
K A, Dill, D, Shortle
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The denatured "state" of a protein is a distribution of many different molecular conformations, the averages of which are measured by experiments. The properties of this ensemble depend sensitively on the solution conditions. There is now considerable evidence that even in strong denaturants such as 6M GuHC1 and 9M urea, some structure may remain in ...
K A, Dill, D, Shortle
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Physical Chemistry, Chemical Physics - PCCP, 2019
Surface-specific spectroscopic data has shown that urea undergoes a shift in orientation at protein surfaces in acidic media. Since urea denatures proteins at a wide range of pHs, the variable chemical nature of protein-urea interactions has been used to
Ivan Pires de Oliveira, L. Martínez
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Surface-specific spectroscopic data has shown that urea undergoes a shift in orientation at protein surfaces in acidic media. Since urea denatures proteins at a wide range of pHs, the variable chemical nature of protein-urea interactions has been used to
Ivan Pires de Oliveira, L. Martínez
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Nature, 1957
REPORTING on the influence of freezing-rate on the denaturation of cold-stored fish, Love1 states that organoleptically determined toughness of cod, stored at − 30° C., does not always involve decreased protein solubility.
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REPORTING on the influence of freezing-rate on the denaturation of cold-stored fish, Love1 states that organoleptically determined toughness of cod, stored at − 30° C., does not always involve decreased protein solubility.
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Critical Reviews in Biochemistry and Molecular Biology, 1990
This article summarizes all experimental facts concerning the cold denaturation of single-domain, multi-domain, and multimeric globular proteins in aqueous solutions with and without urea and guanidine hydrochloride. The facts obtained by various experimental techniques are analyzed thermodynamically and it is shown that the cold denaturation is a ...
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This article summarizes all experimental facts concerning the cold denaturation of single-domain, multi-domain, and multimeric globular proteins in aqueous solutions with and without urea and guanidine hydrochloride. The facts obtained by various experimental techniques are analyzed thermodynamically and it is shown that the cold denaturation is a ...
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Nanotube Confinement Denatures Protein Helices
Journal of the American Chemical Society, 2006In striking contrast to simple polymer physics theory, which does not account for solvent effects, we find that physical confinement of solvated biopolymers decreases solvent entropy, which in turn leads to a reduction in the organized structural content of the polymer.
Eric J, Sorin, Vijay S, Pande
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Nonideality and protein thermal denaturation
Biopolymers, 1999We studied the thermal denaturation of eglin c by using CD spectropolarimetry and differential scanning calorimetry (DSC). At low protein concentrations, denaturation is consistent with the classical two-state model. At concentrations greater than several hundred microM, however, the calorimetric enthalpy and the midpoint transition temperature ...
J C, Waldner +3 more
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Protein Denaturant Binding Polynomials
Journal of Protein Chemistry, 2002We show how moments of the denaturant binding distribution function can be extracted from experimental data on the denaturation of a protein as a function of the concentration of denaturant and how in turn these moments can be used to construct the denaturant binding distribution function.
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Analytical Chemistry, 2018
Described here is a mass spectrometry-based proteomics approach for the large-scale analysis of protein-drug interactions. The approach involves the evaluation of ligand-induced protein folding free energy changes (ΔΔ Gf) using chemical denaturation and ...
He Meng, Renze Ma, M. Fitzgerald
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Described here is a mass spectrometry-based proteomics approach for the large-scale analysis of protein-drug interactions. The approach involves the evaluation of ligand-induced protein folding free energy changes (ΔΔ Gf) using chemical denaturation and ...
He Meng, Renze Ma, M. Fitzgerald
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Protein Denaturation and Aggregation
Annals of the New York Academy of Sciences, 2006Abstract: Protein aggregation is a prominent feature of many neurodegenerative diseases, such as Alzheimer's, Huntington's, and Parkinson's diseases, as well as spongiform encephalopathies and systemic amyloidoses. These diseases are sometimes called protein misfolding diseases, but the latter term begs the question of what is the “folded” state of ...
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