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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
Denaturation of Fish Proteins [PDF]
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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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 ...
David Shortle, Ken A. Dill
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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 ...
David Shortle, Ken A. Dill
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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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Is arginine a protein-denaturant?
Protein Expression and Purification, 2005Arginine is a useful solvent additive for many applications, including refolding and solubilization of proteins from insoluble pellets, and suppression of protein aggregation and non-specific adsorption during formulation and purification. However, there is a concern that arginine may be a protein-denaturant, which may limit the expansion of its ...
Matsujiro Ishibashi +5 more
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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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THE FLUORESCENCE OF NATIVE, DENATURED AND REDUCED‐DENATURED PROTEINS*
Photochemistry and Photobiology, 1971Abstract— (1) By excitation at 295 nm tryptophan fluorescence from 17 proteins was examined free of contributions from tyrosine. The tryptophan quantum yields for native proteins were both higher and lower than that of the free amino acid and spanned a 5‐fold range.
L. G. Holmes, M. J. Kronman
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Mechanical Insight into Resistance of Betaine to Urea-Induced Protein Denaturation.
Journal of Physical Chemistry B, 2016It is known that urea can induce protein denaturation that can be inhibited by osmolytes. Yet, experimental explorations on this mechanism at the molecular level are still lacking.
Jiantao Chen +4 more
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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 ...
Jennifer C. Waldner +3 more
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Journal of Physical Chemistry B, 2015
Molecular dynamics simulations are performed to investigate the counteracting effect of trehalose against urea-induced denaturation of S-peptide analogue.
S. Paul, Sandip Paul
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Molecular dynamics simulations are performed to investigate the counteracting effect of trehalose against urea-induced denaturation of S-peptide analogue.
S. Paul, Sandip Paul
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