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Modalities of Protein Denaturation and Nature of Denaturants [PDF]
International Journal of Pharmaceutical Sciences Review and Research, 2021 Denaturation of protein is a biological phenomenon in which a protein loses its native shape due to the breaking or disruption of weak chemical bonds and interactions which makes the protein biologically inactive. It is the process where properly folded proteins formed under physiological conditions is transformed to an unfolded protein under non ...
Vaishali V. Acharya, Pratima Chaudhuri
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PRESSURE AND PROTEIN DENATURATION [PDF]
Journal of Biological Chemistry, 1946 Kinetic analyses have indicated that moderate hydrostatic pressures, up to some 700 atmospheres, oppose reversible and irreversible denaturations of certain enzyme systems, apparent at temperatures above the normal optimum of the enzyme reaction, as well as at lower temperatures in the presence of denaturants such as alcohol (1-4).
Johnson, Frank H., Campbell, Dan H.
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On the Structural Stability and Solvent Denaturation of Proteins [PDF]
Journal of Biological Chemistry, 1970 SUMMARY The effects of urea and various alkyl-substituted ureas on the native conformation of sperm whale myoglobin, horse heart cytochrome c, and ar-chymotrypsinogen were investigated by means of spectral, difference spectral, and optical rotatory dispersion methods. The effectiveness of the ureas as a class of protein denaturants is found to increase
Theodore T. Herskovits +2 more
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Cold and Warm Denaturation of Proteins
Journal of biological physics, 2001 We introduce a simplified protein model where the water degrees of freedom appear explicitly (although in an extremely simplified fashion). Using this model we are able to recover both the warm and the cold protein denaturation within a single framework, while addressing important issues about the structure of model proteins.
Caldarelli, G., Rios, P. De De
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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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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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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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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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New Powerful Protein Denaturant [PDF]
Biophysical Journal, 2013 Traditional denaturants such as urea and guanidinium hydrochloride effectively unfold a variety of proteins in an “all-or-none” fashion. However their high working concentration in combination with the strong absorption below 210 nm make it impossible to measure high quality circular dichroism spectra, which are commonly used to detect changes in ...
Tatyana Perlova +2 more
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The denaturation of proteins [PDF]
Biochemical Journal, 1932 William Cudmore McCullagh Lewis +1 more
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