Precision scanning microcalorimeter for the study of liquids

Privalov, Peter L.; Plotnikov, Valerian; Filimonov, Vladimir V.

doi:10.1016/0021-9614(75)90079-8

Cited by 230 publications

(57 citation statements)

References 7 publications

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“…It has been already reported [14,17] that the stability of the base line position permits evaluation of values for partial heat capacities from scanning calorimetry experiments. The mean value of the partial specific heat capacity, c;, at 20 "C for tRNA"" in the presence of Mg2+ was found to be equal to 0.26 f 0.04cal.K-' .g-'(1.09 f 0 .…”

Section: Resultsmentioning

confidence: 99%

“…Calorimetric experiments were carried out in a scanning microcalorimeter DASM-1M [17] at a heating rate of 1 K min-'. Partial heat capacities were evaluated as outlined elsewhere [19].…”

Section: Methodsmentioning

confidence: 99%

“…The investigations centered on the determination of the variation with temperature of the partial specific heat capacities of the tRNA solutions by direct scanning microcalorimetry [16,17]. These quantities sensitively reflect the complex energetics of thermal unfolding and allow calculation of all relevant thermodynamic parameters.…”

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confidence: 99%

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Calorimetric Investigations on Thermal Stability of tRNAIle (Yeast) and tRNASer (Yeast)

Filimonov¹,

Privalov²,

Hinz

et al. 1976

Eur J Biochem

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Variation with temperature of the partial heat capacities of tRNAIle (yeast) and tRNASer (yeast) has been determined in two buffers at various salt conditions by scanning microcalorimetry. The overall molar transition enthalpy, ΔHt= 320 ± 20 kcal mol−1 (1339 ± 84 kJ mol−1) is identical for the two tRNA species within the limits of experimental error. ΔHt does not show any dependence on the nature of the buffer, nor does' it vary on addition of 1 mM MgCl2 or 150 mM NaCl. Thermal unfolding of the native structure to the random coil cannot adequately be described by a two‐state, concerted transition under the experimental conditions applied in this study, but exhibits a multistep mechanism characterized by sequential unfolding of separable cooperative domains.

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Section: Resultsmentioning

confidence: 99%

“…Calorimetric experiments were carried out in a scanning microcalorimeter DASM-1M [17] at a heating rate of 1 K min-'. Partial heat capacities were evaluated as outlined elsewhere [19].…”

Section: Methodsmentioning

confidence: 99%

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Calorimetric Investigations on Thermal Stability of tRNAIle (Yeast) and tRNASer (Yeast)

Filimonov¹,

Privalov²,

Hinz

et al. 1976

Eur J Biochem

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“…Calorimetric measurements were performed using high-sensitivity DASM-1M and DASM-4 differential adiabatic scanning microcalorimeters [25]. Sample concentrations between 1 and 5 mg/ml were used.…”

Section: Methodsmentioning

confidence: 99%

Thermal stability of lipid‐depleted purple membranes at neutral and low pH values

1994

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Differential scanning calorimetry was used to compare the thermal behavior of native and delipidated purple membrane fragments at pH values corresponding to purple, blue and acid-purple forms. At neutral pH, delipidation results in a 2.5-to 3-times increase in the cooperativity of the denaturational transition, accompanied by a minor increase in its temperature. At pH values below 5 the delipidated membranes exhibit considerably higher thermal stability than the native membranes. The reversible predenaturational transition observed in the native state is not detectable upon delipidation. There is no strict correlation between color changes upon acid&cation and deionization of either native or delipidated purple membranes and their thermal stability.

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“…Calorimetric experiments were carried out in a high-sensitivity DSC DASM-1M [18] at a heating rate of 0.5 K/min. DSC thermodynamic parameters were calculated as in [lo].…”

Section: Methodsmentioning

confidence: 99%

Reversible thermal transition of brain myelin proteolipid

et al. 1986

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Brain myelin proteolipid has been investigated using high-sensitivity differential scanning calorimetry (DSC) under various conditions. Crude proteolipid with a 40% (w/w) content of protein gave rise to a reversible transition, centered at about 60°C. The specific enthalpy of the transition was 505 5 J.g-' with a calorimetric to van? Hoff enthalpy ratio of 5.7f0.5. To our knowledge this is the first intrinsic membrane protein in which a reversible thermal transition has been detected and investigated by DSC. Similar experiments were carried out using the recombinants of delipidated proteolipid and the pool of natural membrane lipids; in this case the transition was less enthalpic and showed lower cooperativity. The recombinants with lecithins, however, did not show any transition at 60°C. MyelinBasic protein Proteolipid DSC

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Precision scanning microcalorimeter for the study of liquids

Cited by 230 publications

References 7 publications

Calorimetric Investigations on Thermal Stability of tRNAIle (Yeast) and tRNASer (Yeast)

Calorimetric Investigations on Thermal Stability of tRNAIle (Yeast) and tRNASer (Yeast)

Thermal stability of lipid‐depleted purple membranes at neutral and low pH values

Reversible thermal transition of brain myelin proteolipid

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