Výsledky vyhledávání

Thermal properties of intact nucleoproteides

Autor: G. Sh. Chitadze, G. V. Madjagaladze, Chanchalashvili Zi, J. Monaselidze, Mgeladze Gn

Publikováno v: Journal of Polymer Science: Polymer Symposia. 69:17-20

It is established that the process of chromatin melting in tissues proceeds in one stage with the following transition parameters: T = 82°C, Δ T = 7°C, and Q = 24 cal/g DNA. The difference between the heats of melting for chromatin and DNA is 12 c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::06edcd3de90eb5afe2036ac9f4e85c38
https://doi.org/10.1002/polc.5070690105

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Manifestation of intraglobular dynamics at microcalorimetry of leghemoglobin crystals

Autor: Mgeladze Gn, Monaselidze Dr, Esipova Ng, Alexander A. Makarov

Publikováno v: Journal of Polymer Science: Polymer Symposia. 69:101-109

Differential scanning microcalorimetry and microscopy have been used to study thermal transitions in leghemoglobin crystals. It is observed that leghemoglobin crystals do not melt and that their lattices disappear because of denaturation of protein g

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f2e0dd4a3242105c28ea9770ac95674e
https://doi.org/10.1002/polc.5070690115

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Microcalorimetric investigation of dilute and concentrated solutions and films of the polydeoxynucleotide poly[d(A-T)·d(A-T)]

Autor: J. Monaselidze, Mgeladze Gn, E. L. Andronikashvili, A. G. Lezius

Publikováno v: Biopolymers. 13:1751-1756

Microcalorimetric heat capacity measurements on dilute and concentrated solutions and films of poly[d(A-T)·d(A-T)] in 2 M sodium chloride have been carried out. Values for enthalpy, entropy, and temperature of the helix–coil transition have been f

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd29fe8df411e25d6f74a448c606c1f3
https://doi.org/10.1002/bip.1974.360130908

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Microcalorimetry of thermal denaturation of pepsin and trypsin in the crystal state

Autor: Esipova Ng, Mgeladze Gn, Monaselidze Dr, I.P. Kuranova, G.V. Madzhagaladze, A.I. Grebenko, Alexander A. Makarov

Publikováno v: Biochimica et Biophysica Acta (BBA) - Protein Structure. 434:286-289

Heating of pepsin and trypsin crystals was studied by scanning microcalorimetry. A sharp decrease in temperature, halfwidth and heat of transition with a decrease in heating rate was discovered. It was shown that thermal transition is connected only

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::332f8117aa8a9b90205dd73ca0dc552b
https://doi.org/10.1016/0005-2795(76)90060-x

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