The interaction of tubulin and other proteins with structure-stabilizing solvents

Timasheff, Serge N.; Lee, James C.; Pittz, Eugene P.; Tweedy, Neil

doi:10.1016/0021-9797(76)90076-x

Cited by 124 publications

(65 citation statements)

References 20 publications

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“…Because the preferential binding parameter is the extent of "binding" of the ligand (PEG) to the protein measured in a dialysis equilibrium experiment, the exclusion of solvent components from the protein domain is equivalent to an excess of water in the domain of the protein, i.e., to preferential hydration of the protein. The two parameters are related by (Timasheff & Kronman, 1959;Timasheff, 1963) The values listed in column 6 of Tables 1 and 2 are seen to be increasingly positive with an increase in the PEG molecular weight. They attain magnitudes much higher than the usual protein hydration, which is 0.2-0.4 g/g (Bull & Breese, 1968;Kuntz, 1971).…”

Section: Resultsmentioning

confidence: 99%

“…As a consequence, preferential interactions in the presence of sugars are determined strictly by the surface area of the protein (Lee & Timasheff, 1981). Because for BSA the proteinsolvent interfacial area is larger at pH 3.0 than at pH 6.0, the interaction between glucose and the expanded BSA molecule is thermodynamically much more unfavorable at the lower pH (Timasheff et al, 1976). This is manifested by the increase in preferential hydration.…”

Section: As Well As the Appendix Of Arakawa Et Al (1990a)mentioning

confidence: 99%

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Steric exclusion is the principal source of the preferential hydration of proteins in the presence of polyethylene glycols

1992

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The preferential interactions of bovine serum albumin, lysozyme, chymotrypsinogen, ribonuclease A, and 6-lactoglobulin with polyethylene glycols (PEGS) of molecular weight 200-6,OOO have been measured by dialysis equilibrium coupled with high precision densimetry. All the proteins were found to be preferentially hydrated in all the PEGs, and the magnitude of the preferential hydration increased with increasing PEG size for each protein.The change in the chemical potentials of the proteins with the addition of the PEGs had highly positive values, indicating a strong thermodynamic destabilization of the system by the PEGs. A viscosity study of the PEGs showed them to be randomly coiled polymers, as their radii of gyration were related to the molecular weight by R, = a M 0 , 5 s . The thickness of the effective shell impenetrable to PEG around protein molecules, calculated from the preferential hydration, was found to vary with PEG molecular weight in similar fashion as the PEG radius of gyration, supporting the proposal (Arakawa, T. & Timasheff, S.N., 1985a, Biochemistry 24,6756-6762) that the preferential exclusion of PEGs from proteins is due principally to the steric exclusion of PEG from the protein domain, although favorable interactions with protein surface residues, in particular nonpolar ones, may compete with the exclusion. These thermodynamically unfavorable preferential exclusion interactions lead to the action of PEGs as precipitants, although they may destabilize protein structure at higher temperatures.

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Section: Resultsmentioning

confidence: 99%

Section: As Well As the Appendix Of Arakawa Et Al (1990a)mentioning

confidence: 99%

Steric exclusion is the principal source of the preferential hydration of proteins in the presence of polyethylene glycols

1992

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“…However, pressure-temperature phase diagrams of integral membrane proteins in phosphilipid bilayers that could provide experimental evidence for this hypothesis are currently not available. Addition of disaccharides to biological systems protects against changes in the physical state of membrane lipids and maintains the native structure of proteins during physical and chemical stresses (9,10,18,37,45). Timasheff et al (37) have suggested that stabilization of proteins in sugar solutions is due to the preferential exclusion of the sugar from contact with the protein surface.…”

Section: Discussionmentioning

confidence: 99%

“…Addition of disaccharides to biological systems protects against changes in the physical state of membrane lipids and maintains the native structure of proteins during physical and chemical stresses (9,10,18,37,45). Timasheff et al (37) have suggested that stabilization of proteins in sugar solutions is due to the preferential exclusion of the sugar from contact with the protein surface. The native protein structure is stabilized because denaturation of the protein molecule leads to a larger contact surface between the protein and the solvent and therefore enhances this thermodynamically unfavorable effect.…”

Section: Discussionmentioning

confidence: 99%

Protective Effect of Sucrose and Sodium Chloride for Lactococcus lactis during Sublethal and Lethal High-Pressure Treatments

Molina-Höppner

Doster

Vogel

et al. 2004

Appl Environ Microbiol

172

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The bactericidal effect of hydrostatic pressure is reduced when bacteria are suspended in media with high osmolarity. To elucidate mechanisms responsible for the baroprotective effect of ionic and nonionic solutes, Lactococcus lactis was treated with pressures ranging from 200 to 600 MPa in a low-osmolarity buffer or with buffer containing 0.5 M sucrose or 4 M NaCl. Pressure-treated cells were characterized in order to determine viability, the transmembrane difference in pH (⌬pH), and multiple-drug-resistance (MDR) transport activity. Furthermore, pressure effects on the intracellular pH and the fluidity of the membrane were determined during pressure treatment. In the presence of external sucrose and NaCl, high intracellular levels of sucrose and lactose, respectively, were accumulated by L. lactis; 4 M NaCl and, to a lesser extent, 0.5 M sucrose provided protection against pressure-induced cell death. The transmembrane ⌬pH was reversibly dissipated during pressure treatment in any buffer system. Sucrose but not NaCl prevented the irreversible inactivation of enzymes involved in pH homeostasis and MDR transport activity. In the presence 0.5 M sucrose or 4 M NaCl, the fluidity of the cytoplasmic membrane was maintained even at low temperatures and high pressure. These results indicate that disaccharides protect microorganisms against pressure-induced inactivation of vital cellular components. The protective effect of ionic solutes relies on the intracellular accumulation of compatible solutes as a response to the osmotic stress. Thus, ionic solutes provide only asymmetric protection, and baroprotection with ionic solutes requires higher concentrations of the osmolytes than of disaccharides.The accumulation of compatible solutes, such as betaines, proline, and sugars, is a widespread response of microorganisms to elevated environmental osmotic pressures (41). According to a recent definition, a compatible solute is a "cytoplasmic cosolvent (solute) whose levels can be modulated over a broad range without disrupting cellular function" (24, 43). Compatible solutes contribute to the osmotic balance with the extracellular environment, enhance the stability of enzymes, and preserve the integrity of biological membranes (41). The composition of the osmolytes that are accumulated depends on the type of osmotic shock (i.e., ionic stress versus nonionic stress) and the presence of specific compatible solutes in the medium. In addition to their role as osmotic balancers, compatible solutes provide protection against high temperature, freeze-thaw treatment, and drying (41, 43).When the osmotic pressure of the medium is increased, the tolerance of microorganisms to high hydrostatic pressure is enhanced. Baroprotective effects of sodium chloride or sugars have been observed in studies with Escherichia coli, Saccharomyces cerevisiae, Zygosaccharomyces spp., and Rhodoturula rubra (14,17,24,25,36). The influence of salts or sugars on the water activity (a w ) of foods or suspension media does not explain the marked baroprotectiv...

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“…A high concentration of additive will be necessary to achieve a reasonable range of density and it cannot then be assumed that preferential exclusion of solute from the incorporated solvent would be a negligible factor (10,11). This would require the addition of another term in Eq.…”

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confidence: 99%

Determination of molecular weight of the protein moiety in protein-detergent complexes without direct knowledge of detergent binding.

Reynolds¹,

Tanford²

1976

Proc. Natl. Acad. Sci. U.S.A.

131

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Sedimentation equilibrium measurements can be used to determine the molecular weight of the protein moiety of a protein-detergent complex without prior knowledge of detergent binding. The procedure is to adjust the solvent density by addition of D20 so as to blank out the contribution of bound detergent to the sedimentation potential. An approximate measure of detergent binding can be obtained from the effect of solvent density on the sedimentation result. The procedure is also applicable to protein-lipid complexes. It The purpose of this paper is to show that the difficulty created by inability to determine the amount of bound detergent can be circumvented by using D20 to adjust the density of the solvent to the point where it matches the buoyant density of the detergent. The detergent then makes no contribution to the sedimentation potential, no matter how much is bound. partial specific volume. Their purpose was different from ours, but the underlying physical principle is the same. D20 has been used to blank out the detergent contribution in neutron scattering by protein-detergent complexes (5), and sucrose has been used for the same purpose in x-ray scattering (6).THEORETICAL BASIS Treatment of sedimentation equilibrium in terms of the thermodynamics of multicomponent solutions (7)

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The interaction of tubulin and other proteins with structure-stabilizing solvents

Cited by 124 publications

References 20 publications

Steric exclusion is the principal source of the preferential hydration of proteins in the presence of polyethylene glycols

Steric exclusion is the principal source of the preferential hydration of proteins in the presence of polyethylene glycols

Protective Effect of Sucrose and Sodium Chloride for Lactococcus lactis during Sublethal and Lethal High-Pressure Treatments

Determination of molecular weight of the protein moiety in protein-detergent complexes without direct knowledge of detergent binding.

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