Forces between hydrophobic surfaces in aqueous electrolyte and surfactant solutions containing common air-borne impurities

Israelachvili, Jacob N.; Pashley, Richard M.; Perez, Éric; Tandon, Rajan

doi:10.1016/0166-6622(81)80016-9

Cited by 34 publications

(22 citation statements)

References 10 publications

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“…Of particular interest are the force spectroscopy measurements of ⌬x which provide a direct measure of the length scales of a transition state, which were hitherto unknown. For example, for protein folding the distance to the folding transition state, ⌬x f , was found to be between 8 Å (17) and 60 Å (23), in rough agreement with the expected role of long range hydrophobic forces (24). For protein unfolding ⌬x u was found to be much shorter, in the range of 1.7-2.5 Å (16,19,21).…”

mentioning

confidence: 52%

RETRACTED: Solvent molecules bridge the mechanical unfolding transition state of a protein

Dougan

Feng

Lü

et al. 2008

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

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We demonstrate a combination of single molecule force spectroscopy and solvent substitution that captures the presence of solvent molecules in the transition state structure. We measure the effect of solvent substitution on the rate of unfolding of the I27 titin module, placed under a constant stretching force. From the force dependency of the unfolding rate, we determine Δ x u , the distance to the transition state. Unfolding the I27 protein in water gives a Δ x u = 2.5 Å, a distance that compares well to the size of a water molecule. Although the height of the activation energy barrier to unfolding is greatly increased in both glycerol and deuterium oxide solutions, Δ x u depends on the size of the solvent molecules. Upon replacement of water by increasing amounts of the larger glycerol molecules, Δ x u increases rapidly and plateaus at its maximum value of 4.4 Å. In contrast, replacement of water by the similarly sized deuterium oxide does not change the value of Δ x u . From these results we estimate that six to eight water molecules form part of the unfolding transition state structure of the I27 protein, and that the presence of just one glycerol molecule in the transition state is enough to lengthen Δ x u . Our results show that solvent composition is important for the mechanical function of proteins. Furthermore, given that solvent composition is actively regulated in vivo , it may represent an important modulatory pathway for the regulation of tissue elasticity and other important functions in cellular mechanics.

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mentioning

confidence: 52%

RETRACTED: Solvent molecules bridge the mechanical unfolding transition state of a protein

Dougan

Feng

Lü

et al. 2008

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

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“…The values of constants used in the calculation of X-DLVO potentials are listed in Table 5 (Israelachvili, 2011;Israelachvili et al, 1981;Pandya et al, 1998;Verwey and Overbeek, 1948;Yukselen and Kaya, 2003). Fig.…”

Section: Calculation Of Extended Dlvo (X-dlvo) Potentials Between a Fmentioning

confidence: 99%

“…λ is the thickness of the formed layer around the charged surfaces in contact with water (0.3 nm for 1:1 electrolytes and 0.18 nm for 2:1 electrolytes) (Israelachvili, 2011;Israelachvili et al, 1981) and for acid-base interactions in water 0.6 nm was offered by Van Oss, κ is the inverse Debye screening length, and p ξ and s ξ are the surface potentials of the particle and silica surfaces respectively. It should be mentioned that 1:1 electrolyte means the cation to anion charge ratio is 1, such as monovalent salts like NaCl and KCl and 2:1 electrolyte means the ratio of cation to anion charge is 2 like CaCl 2 and MgCl 2 .…”

Section: Calculation Of Extended Dlvo (X-dlvo) Potentials Between a Fmentioning

confidence: 99%

Application of nanofluid to control fines migration to improve the performance of low salinity water flooding and alkaline flooding

Assef

Arab

Pourafshary

2014

Journal of Petroleum Science and Engineering

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“…The surface structural forces arising upon interaction between objects consisting of quartz and silica glass are most extensively studied. The intensity parameter and the correlation length for the quartz surface are as follows: K = (1-2) × 10 6 J/m 3 and l = 1-1.6 nm in the one-term isotherm [formula (6)] [14,35,36]. However, in our earlier work [37], we estimated the parameters of the structural component V s for different pH values and revealed that, at the isoelectric point, the parameters K and l are considerably larger and, correspondingly, the boundary layers are more extended.…”

Section: Investigation Of Electrical Surface Properties Of Particlesmentioning

confidence: 99%

Aggregate stability of ZrO2 aqueous sols in electrolyte solutions

et al. 2008

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The aggregate stability of submicron and nanosized ZrO 2 aqueous sols of different origins and different dispersities at pH 3-10 in the KCl concentration range 10 -3 -10 -1 M is investigated by flow ultramicroscopy and photometry. The results obtained are analyzed in the framework of the extended Derjaguin-Landau-Verwey-Overbeek theory and the Muller-Martynov theory of reversible aggregation. The extension of boundary layers of water near the surface of the ZrO 2 particles is estimated.

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Forces between hydrophobic surfaces in aqueous electrolyte and surfactant solutions containing common air-borne impurities

Cited by 34 publications

References 10 publications

RETRACTED: Solvent molecules bridge the mechanical unfolding transition state of a protein

RETRACTED: Solvent molecules bridge the mechanical unfolding transition state of a protein

Application of nanofluid to control fines migration to improve the performance of low salinity water flooding and alkaline flooding

Aggregate stability of ZrO2 aqueous sols in electrolyte solutions

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