On the average hydrophobicity of proteins and the relation between it and protein structure

Bigelow, Charles C.

doi:10.1016/0022-5193(67)90004-5

Cited by 784 publications

(256 citation statements)

References 43 publications

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“…Notably, Bigelow [20] [23,24]. Separation is commonly carried out under denaturing conditions using organic solvents, which may result, in an unpredictable fashion, in the exposure of the internal residues of the protein to the matrix.…”

Section: Discussionmentioning

confidence: 99%

Spectrofluorimetric assessment of the surface hydrophobicity of proteins

Cardamone

Puri²

1992

Biochemical Journal

462

305

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The equilibrium binding of the apolar fluorescent dye l-anilinonaphthalene-8-sulphonate (ANS) to bacteriorhodopsin, BSA, chicken egg lysozyme, ovalbumin, porcine somatotrophin (PST) and bovine pancreatic ribonuclease (RNAase) was quantitatively evaluated using Scatchard-and Klotz-plot analyses. On the basis of the average association constant for ANS binding sites (Ka), the proteins could be ranked in order of surface hydrophobicity as:Bacteriorhodopsin > BSA > ovalbumin > PST > lysozyme > RNAase

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Section: Discussionmentioning

confidence: 99%

Spectrofluorimetric assessment of the surface hydrophobicity of proteins

Cardamone

Puri²

1992

Biochemical Journal

462

305

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“…This can be considered in light of Equation 4, i.e., the decomposition of the preferential interaction (thermodynamic binding) into contacts at protein surface loci of water and sorbitol molecules, respectively. Ribonuclease has a high ratio of polar amino acid residues to nonpolar ones (1.73) and a very low hydrophobicity (Bigelow, 1967). With such a high polarity, RNase A has a very hydrophilic surface.…”

Section: Why Is Sorbitol Preferentially Excluded?mentioning

confidence: 99%

Mechanism of the stabilization of ribonuclease a by sorbitol: Preferential hydration is greater for the denatured than for the native protein

1997

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The effect of interactions of sorbitol with ribonuclease A (RNase A) and the resulting stabilization of structure was examined in parallel thermal unfolding and preferential binding studies with the application of multicomponent thermodynamic theory. The protein was stabilized by sorbitol both at pH 2.0 and pH 5.5 as the transition temperature, Tm, was increased. The enthalpy of the thermal denaturation had a small dependence on sorbitol concentration, which was reflected in the values of the standard free energy change of denaturation, SAG" = AC"(sorbito1) -AG"(water). Measurements of preferential interactions at 48 "C at pH 5.5, where protein is native, and pH 2.0, where it is denatured, showed that sorbitol is preferentially excluded from the denatured protein up to 40%, but becomes preferentially bound to native protein above 20% sorbitol. The chemical potential change on transferring the denatured RNase A from water to sorbitol solution is larger than that for the native protein, A p f > A&, which is consistent with the effect of sorbitol on the free energy change of denaturation. The conformity of these results to the thermodynamic expression of the effect of a co-solvent on denaturation, AG; + A p f = AG; + A p f , indicates that the stabilization of the protein by sorbitol can be fully accounted for by weak thermodynamic interactions at the protein surface that involve water co-solvent exchange at thermodynamically non-neutral sites. The protein structure stabilizing action of sorbitol is driven by stronger exclusion from the unfolded protein than from the native structure.

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“…1B), and their peptidic composition, presented in Table 2, showed that most larger peptides were rejected by PES-1, HYD-2 and PES-5 membranes, whereas those having a molecular mass lower than 1 kDa were mainly transmitted to the permeate stream. In contrast, the chromatographic profile corresponding to the DR sample showed an Bigelow (1967).…”

Section: Peptidic Composition Of the B-lg Fractionsmentioning

confidence: 73%