Partial heat capacity change — Fundamental characteristic of the process of thermal denaturation of biological macromolecules (proteins and nucleic acids)

Mrevlishvili, G. M.; Metreveli, Nunu; Razmadze, G. Z.; Mdzinarashvili, Tamaz; Kakabadze, G.R.; Khvedelidze, Mariam

doi:10.1016/s0040-6031(97)00328-6

Cited by 16 publications

(12 citation statements)

References 14 publications

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“…Figure 5 plots the melting time versus the total number of dissociated basepairs in 11 bp at different ionic concentrations. It shows that the DNA melting time becomes shorter in a saline solution with lower ionic concentration, namely a higher melting speed can be achieved by reducing the saline concentration, which elucidates that the stability of DNA can be improved by elevating the ionic concentration, and this trend is likely related to the positive correlation between thermo-stability of dsDNA and ionic concentration as discovered in experiments (Sorokin et al 1997 ; Mrevlishvili et al 1998 ). Indeed, the addition of ions can screen the electrostatic interaction between phosphate groups in two strands of dsDNA, leading to the improvement of DNA stability.…”

Section: Resultsmentioning

confidence: 75%

“…The concentration of salt plays an important role in DNA melting profile (Sorokin et al 1997 ; Mrevlishvili et al 1998 ), and one can expect the ionic concentration can affect the melting pathway as well. Figure 5 plots the melting time versus the total number of dissociated basepairs in 11 bp at different ionic concentrations.…”

Section: Resultsmentioning

confidence: 99%

“…The melting temperature is closely related to the environment to which the DNA is subjected (Sorokin et al 1997 ; Mrevlishvili et al 1998 ; Goobes et al 2003 ; Khimji et al 2013 ; Nakano et al 2014 ). Mrevlishvili et al (Mrevlishvili et al 1998 ) found that the DNA melting temperature increases with the increase of the ionic concentration, and the same conclusion has been drawn by Sorokin et al through a study on the influences of ions on the thermo-stability of dsDNA (Sorokin et al 1997 ). Goobes et al ( 2003 ) added crowding reagent PEG into DNA solution, and found that inertia polymers are in favor with the thermostability of DNA.…”

Section: Introductionmentioning

confidence: 99%

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Melting dynamics of short dsDNA chains in saline solutions

Shang

Liu

et al. 2015

SpringerPlus

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DNA melting has attracted much attention due to its importance in understanding the life-reproduction and metabolism and in the applications of modern DNA-based technologies. While numerous works have been contributed to the determination of melting profiles in diverse environments, the understanding of DNA melting dynamics is still limited. By employing three-site-per-nucleotide (3SPN) double-stranded DNA (dsDNA) model, we here demonstrate the melting dynamics of an isolated short dsDNA under different conditions (different temperatures, ionic concentrations and DNA chain lengths) can be accessed by coarse-grained simulation studies. We particularly show that at dilute ionic concentration the dsDNA, regardless being symmetric or asymmetric, opens at both ends with roughly equal probabilities, while at high ionic concentration the asymmetric dsDNA chain opens at the A-T-rich end. The comparisons of our simulation results to available data are discussed, and overall good agreements have been found.

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Section: Resultsmentioning

confidence: 75%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Melting dynamics of short dsDNA chains in saline solutions

Shang

Liu

et al. 2015

SpringerPlus

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“…In the meanwhile, Meanwhile, Mrevlishvil [197] and Goldanskii et al [198] measured the speci ic heat of various biopolymers including proteins and DNA. They obtained…”

Section: The Evidences Of Specifi C Heat Of Acetanilide and Proteinsmentioning

confidence: 99%

“…For Pang' solution model in protein molecules the solution solutions are denoted by Equation (45)- (46). In this case the energy of the supersound solution or 50is consistent with Meanwhile, Mrevlishvil and Goldanskii et al experimental data in proteins and DNA [197][198][199][200].…”

Section: The Evidences Of Specifi C Heat Of Acetanilide and Proteinsmentioning

confidence: 99%

The bio-energy transport in the protein molecules and its experimental validations of correctness

Pang¹

2017

Ann Proteom Bioinform

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The bio-energy released by the hydrolysis of adenosine triphosphate, which relate to plenty of life activities and is transported in a solution, and its theory of transport are fi rst stated and built in helix protein molecule. In order to confi rm and verify the correctness of the transported theory we here systematically summarized and reviewed a great number of experimental investigation and evidences obtained by us and other researchers in past 30 years, involving the real existences of the solution and its features and lifetimes. In this survey we outlined and presented concretely the features of infrared spectra of absorption, Raman spectra and specifi c heat of the molecular crystal-acetanilide collagen, bivine serum albumin, myoglobin proteins and E.Coli. cell as well as the lifetimes of the solution in acetanilide and myoglobin measured by using pump-probe techniques and free-electron laser experiment, in which we give not only experimental data but also their comparisons with theoretical results. These experimental data and evidences provided here are enough to verify and affi rm the true existences of the new solution, which can complete itself functions of bio-energy transport in the lifetime, and the correctness of the new theory of bio-energy transport in the acetanilide and protein molecule. Thus we can affi rm the correctness of theory of the bio-energy transport in helix protein molecule, which can greatly promote the development of molecular biology.

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Thermal behavior of modern and archeological enamel and dentin by in situ temperature‐dependent Raman spectroscopy

Киселева

Pankrushina

2023

J Raman Spectroscopy

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Teeth and bones are important bioarchives, which can be altered because of diagenesis or burning (cooking, funerary cremations, and fires). Though heating and diagenesis are different processes, an experimental heating of modern bioapatite reproduces in a short time effects similar to diagenetic processes occurring over geological time. The thermal behavior of modern and archeological human enamel and dentin using the in situ thermo-Raman spectroscopy at 83-873 K was investigated to assess the structural changes in organic and mineral components of a tooth and their interrelationship. The ν 1 (PO 4 ) vibrational mode in apatite is the most anharmonic and responsible for the reaction of the structure to external influences. The γiP isobaric Grüneisen parameters for archeological (0.41) and modern (0.24) enamel are different from those for fluor-(0.17) and chlorapatite (0.17), which indicates a stronger reaction of P O bonds in bioapatite PO4 tetrahedra to temperature changes as compared with geologic samples. The anomalies of the thermal dependences of the ν 1 (PO 4 ) peak position and Δcorr PO 4 (T) autocorrelation function are caused by the combined effect of different factors such as breaking of hydroxyl and hydrogen bonds, the loss of adsorbed and structural water, collagen denaturation, organic phase combustion, and removal and relocation of B-and A-type carbonate ions. The thermal (273, 313, 341, and 363 K) and cold ($160 K) denaturation of collagen is reflected in the ν 1 (PO 4 ) and Δcorr PO 4 (T) dependences. The Δcorr PO 4 (T) differences between modern and archeological dentin and enamel are contingent on bioapatite composition (proportions of adsorbed and structural water, hydroxyl and carbonate ions, and trace elements as well as different types of organic matterlowmolecular noncollagen compounds and high-molecular collagen). The results obtained contribute to the knowledge about the thermal transformations of the mineral and organic phases of modern and archeological tooth tissues and allow their structural alterations to be evaluated.

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Partial heat capacity change — Fundamental characteristic of the process of thermal denaturation of biological macromolecules (proteins and nucleic acids)

Cited by 16 publications

References 14 publications

Melting dynamics of short dsDNA chains in saline solutions

Melting dynamics of short dsDNA chains in saline solutions

The bio-energy transport in the protein molecules and its experimental validations of correctness

Thermal behavior of modern and archeological enamel and dentin by in situ temperature‐dependent Raman spectroscopy

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