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Acoustic probing of new biomarkers for rapid sickle cell disease screening.
Sridhar N +4 more
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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 ...
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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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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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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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.
M. J. KRONMAN, L. G. HOLMES
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