Properties of amides in aqueous solution. I. Viscosity and density changes of amide-water systems. An analysis of volume deficiencies of mixtures based on molecular size differences (mixing of hard spheres)

Assarsson, P.; Eirich, F. R.

doi:10.1021/j100854a004

Cited by 254 publications

(97 citation statements)

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“…3H20. These are in agreement with the findings of other workers (6,9,12,14) who have studied the same solvent mixture through other properties. From the curve -q VS. solvent composition, it is clear that the effect of the addition of DMF to water is more pronounced than that of the addition of water to DMF as indicated by the rate of change of viscosity.…”

Section: Resultssupporting

confidence: 93%

Conductance studies in amide–water mixtures. VI. Nitrates of sodium, potassium, and ammonium in N,N-dimethylformamide–water mixtures at 25 °C

Bahadur¹,

Ramanamurti²

1984

Can. J. Chem.

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LAL BAHADUR and M. V. RAMANAMURTI. Can. J. Chem. 62, 1051 (1984. Conductance data for the nitrates of sodium, potassium, and ammonium in N,N-dimethylformamide (DMF) -water mixtures (74.39 2 D 2 36.11) at 25°C are reported for the concentration range 0.0003-0.06 mol dm-,. Also densities, viscosities, and dielectric constants of the solvent mixture (DMF-water) are reported at the same temperature. The data have been analysed by the Fuoss (1978) equation excluding the term a. The existence of a maximum in the viscosity at a 1 : 3 mol ratio of DMF and water is attributed to the formation of a solvated complex DMF. 3Hz0. The Walden products for all the three salts pass through a maximum while the equivalent conductances show a minimum with the change of DMF content in the solvent mixtures. In any given solvent mixture, the limiting equivalent conductances show the trend NaNO, < KNO, < NH4N03.

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Section: Resultssupporting

confidence: 93%

Conductance studies in amide–water mixtures. VI. Nitrates of sodium, potassium, and ammonium in N,N-dimethylformamide–water mixtures at 25 °C

Bahadur¹,

Ramanamurti²

1984

Can. J. Chem.

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“…For example, the dilution of pure dimethylacetamide in a continuum solvent results in a 30% decrease in specific volume (Assarsson & Eirich, 1968). Weber and Drickamer (1983) predict these packing defects to provide the major contribution to the value of AV,.…”

Section: Kj F T Y and Ca Royermentioning

confidence: 99%

Probing the contribution of internal cavities to the volume change of protein unfolding under pressure

Frye¹,

Royer²

1998

Protein Science

145

129

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The structural origin of the decrease in system volume upon protein denaturation by pressure has remained a puzzle for decades. This negative volume change upon unfolding is assumed to arise globally from more intimate interactions between the polypeptide chain and water, including electrostriction of buried charges that become exposed upon unfolding, hydration of the polypeptide backbone and amino acid side chains and elimination of packing defects and internal void volumes upon unfolding of the chain. However, the relative signs and magnitudes of each of these contributing factors have not been experimentally determined. Our laboratory has probed the fundamental basis for the volume change upon unfolding of staphylococcal nuclease (Snase) using variable solution conditions and point mutants of Snase (Royer CA et al., 1993, Biochemistry 325222-5232; Frye KJ et al., 1996, Biochemistry 35:10234-10239). Our prior results indicate that for Snase, neither electrostriction nor polar or nonpolar hydration contributes significantly to the value of the volume change of unfolding. In the present work, we investigate the pressure induced unfolding of three point mutants of Snase in which internal cavity size is altered. The experimentally determined volume changes of unfolding for the mutants suggest that loss of internal void volume upon unfolding represents the major contributing factor to the value of the volume change of Snase unfolding.Keywords: high pressure; protein folding; staphylococcal nuclease; volume change Understanding protein folding remains one of the most challenging problems in modem molecular biophysics. Considerable progress has been made in the last decade in the characterization of the fundamental thermodynamic and kinetic aspects of the process, as well as in the structural characterization of the various states, native, intermediate, and unfolded, implicated in the transitions. From a thermodynamic point of view, the fundamental parameter in protein temperature stability, the heat capacity change at constant pressure, which is responsible for the temperature dependence of the entropy, enthalpy, and free energy of folding, has been parameterized and can now be modeled adequately, in terms of the changes in exposure of hydrophobic and hydrophilic moieties of particular proteins based on their sequences and structures (Privalov & Gill, 1988;Murphy & Freire, 1992).Athorough understanding of the thermodynamics of protein folding requires, in addition to the temperature effects, a fundamental comprehension of pressure effects as well. However, in terms of the behavior of proteins under pressure, our level of understanding is much less advanced than in the field of temperature denaturation. (For reviews of pressure effects on proteins see Jaenicke, 1981; HerReprint requests to: Catherine A. Royer, Centre de Biochimie Structurale, INSERM U414, Facultt de Pharmacie, 15 ave. Ch. Flahault, 34060 Montpellier CEDEX, France; e-mail: royer@tome.cbs.univ-montpl.fr. emans, 1982;Weber & Drickamer, 1983;Si...

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“…5) [10]. The minimum value of ΔV at x 2 = 0.33 proves that molecular complexes of the type 2(D-i-PA) : H2O develop in the solutions.…”

Section: Excess Functions Of Mole Volume δVm and Adiabatic Compressibmentioning

confidence: 86%

Investigation of Adiabatic Compressibility and Ultrasonic Relaxation in Aqueous Solutions of N, N-Diisopropylacetamide and Zinc Acetate

Miecznik

1994

Acta Phys. Pol. A

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Measurements of velocity at frequency of 1 MHz and absorption coefficient of ultrasonic waves within the range 3-50 MHz in aqueous solutions of N,N-diisopropylacetamide (D-i-PA) and zinc acetate ((CH3COO)2Zn) were made. Additionally, the density of the solutions was measured. The adopted method for making the solutions helped to change the ratio of the number of non-electrolyte molecules to that of electrolyte molecules, with a constant number of water molecules. Measurements of the velocity of ultrasonic waves in the solutions under study were conducted by means of an impulse-phase interferometer. Measurements of the absorption coefficient of ultrasonic waves were conducted by means of an ultrasonic high frequency system, type Matec Instruments (USA) Model 7700. All the measurements were conducted at a constant temperature of 20°C.

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Properties of amides in aqueous solution. I. Viscosity and density changes of amide-water systems. An analysis of volume deficiencies of mixtures based on molecular size differences (mixing of hard spheres)

Cited by 254 publications

References 1 publication

Conductance studies in amide–water mixtures. VI. Nitrates of sodium, potassium, and ammonium in N,N-dimethylformamide–water mixtures at 25 °C

Conductance studies in amide–water mixtures. VI. Nitrates of sodium, potassium, and ammonium in N,N-dimethylformamide–water mixtures at 25 °C

Probing the contribution of internal cavities to the volume change of protein unfolding under pressure

Investigation of Adiabatic Compressibility and Ultrasonic Relaxation in Aqueous Solutions of N, N-Diisopropylacetamide and Zinc Acetate

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