On the Structural Stability and Solvent Denaturation of Proteins

Herskovits, Theodore T.; Jaillet, Helen; Gadegbeku, Barbara

doi:10.1016/s0021-9258(19)63824-x

Cited by 113 publications

(11 citation statements)

References 40 publications

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“…The large effect of «-butylurea with uric acid contrasts with the small effect of other alkyl substituents (Figure 5); a similar result has been found for protein denaturation. 36 The value of -AGtr of 489 cal/mol is close to the sum of the values for urea and «-butyl alcohol of 214 and 228 cal/mol, respectively, suggesting that the effects of the urea and «-butyl groups of «-butylurea are roughly additive.…”

Section: Discussionmentioning

confidence: 69%

Interactions of urea and other polar compounds in water

Roseman¹,

Jencks²

1975

J. Am. Chem. Soc.

198

121

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Section: Discussionmentioning

confidence: 69%

Interactions of urea and other polar compounds in water

Roseman¹,

Jencks²

1975

J. Am. Chem. Soc.

198

121

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“…Considering that urea shifts optical rotation of proteins to the negative side (more levorotatory) and weakens the hydrophobic interaction of proteins in aqueous solution (Tanford et al, 1960;Brandts & Hunt, 1967; Dubin & Strauss, 1973), the amphiphiles and nonpolar additives enhance hydrophobic interactions. Thus, it is generally accepted that their effect is attributable to the enhancement of hydrophobic interactions among side chains (Tanford & De, 1961;Herskovitz et al, 1970).…”

Section: Discussionmentioning

confidence: 99%

Biphasic effects of alcohols on the phase transition of poly(L-lysine) between .alpha.-helix and .beta.-sheet conformations

Shibata¹,

Yamamoto²,

Yamashita³

et al. 1992

Biochemistry

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Poly(L-lysine) exists as a random-coil at neutral pH, an alpha-helix at alkaline pH, and a beta-sheet when the alpha-helix poly(L-lysine) is heated. The present Fourier-transform infrared (FTIR) study showed that short-chain alcohols (methanol, ethanol, and 2-propanol) partially transformed alpha-helix poly(L-lysine) to beta-sheet when their concentrations were low. At higher concentrations, however, these alcohols reversed the reaction, and the alcohol-induced beta-sheet was transformed back to alpha-helix structure. The reversal occurred at 1.40 M methanol, 0.96 M ethanol, and 0.55 M 2-propanol. The alcohol effects on the secondary structure were further investigated by circular dichroism (CD) on the thermally induced beta-sheet poly(L-lysine). Methanol, ethanol, and 1-propanol, but not 1-butanol, shifted the negative mean-residue ellipticity at 217 nm of the beta-sheet poly(L-lysine) to the positive side at low concentrations of the alcohols and to the negative side at high concentrations. With 1-butanol, only the positive-side shift was observed. The positive-side shift at low concentrations of alcohols indicates enhancement of the hydrophobic interactions among the side chains of the polypeptide in the beta-sheet conformation. The negative-side shift indicates a partial transformation to alpha-helix. The shift from the positive to negative side occurred at 7.1 M methanol, 4.6 M ethanol, and 3.1 M 1-propanol. The alcohol concentrations for the beta-to-alpha transition were higher in the CD study than in the IR study.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…These detergents are not compatible with high amounts of urea [23], so that we tried to replace at least part of the urea by another chaotrope. We first tested chaotropes which were claimed to be at least as efficient as urea, namely substituted ureas [32], formamide and thiourea [33]. Typical results are shown in Figure 2.…”

Section: Preliminary Experiments 2-d Page Of Membrane Proteins With I...mentioning

confidence: 99%

“…Here again, we tried to select chaotropes as powerful as possible. This led us to test mainly alkylureas [32] and thiourea. The latter compound is weakly soluble in water (ca.…”

Section: Tests On Membrane Proteinsmentioning

confidence: 99%

Improvement of the solubilization of proteins in two‐dimensional electrophoresis with immobilized pH gradients

et al. 1997

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Membrane and nuclear proteins of poor solubility have been separated by high resolution two-dimensional (2-D) gel electrophoresis. Isoelectric focusing with immobilized pH gradients leads to severe quantitative losses of proteins in the resulting 2-D map, although the resolution is usually high. Protein solubility could be improved by using denaturing solutions containing various detergents and chaotropes. Best results were obtained with a denaturing solution containing urea, thiourea, and detergents (both nonionic and zwitterionic). The usefulness of thiourea-containing denaturing mixtures is shown for microsomal and nuclear proteins as well as for tubulin, a protein highly prone to aggregation.

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On the Structural Stability and Solvent Denaturation of Proteins

Cited by 113 publications

References 40 publications

Interactions of urea and other polar compounds in water

Interactions of urea and other polar compounds in water

Biphasic effects of alcohols on the phase transition of poly(L-lysine) between .alpha.-helix and .beta.-sheet conformations

Improvement of the solubilization of proteins in two‐dimensional electrophoresis with immobilized pH gradients

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