Results 241 to 250 of about 196,670 (297)

Thymus deoxyribonucleoproteinIV. Thermal denaturation

Biochimica et Biophysica Acta, 1963
Abstract The effects of thermal denaturation on the ultraviolet absorption and viscosity of calf-thymus deoxyribonucleohistone and deoxyribonucleic acid have been compared. The denaturation temperature of nucleohistone was higher than that of nucleic acid.
M F, LEE, I O, WALKER, A R, PEACOCKE
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Nonideality and protein thermal denaturation

Biopolymers, 1999
We studied the thermal denaturation of eglin c by using CD spectropolarimetry and differential scanning calorimetry (DSC). At low protein concentrations, denaturation is consistent with the classical two-state model. At concentrations greater than several hundred microM, however, the calorimetric enthalpy and the midpoint transition temperature ...
J C, Waldner, S J, Lahr, M H, Edgell, G J, Pielak   +3 more
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Thermal denaturation of staphylococcal nuclease

Biochemistry, 1985
The fully reversible thermal denaturation of staphylococcal nuclease in the absence and presence of Ca2+ and/or thymidine 3',5'-diphosphate (pdTp) from pH 4 to 8 has been studied by high-sensitivity differential scanning calorimetry. In the absence of ligands, the denaturation is accompanied by an enthalpy change of 4.25 cal g-1 and an increase in ...
R O, Calderon, N J, Stolowich, J A, Gerlt, J M, Sturtevant   +3 more
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Thermal denaturation of subchromosomal particles

Biochemical and Biophysical Research Communications, 1975
Summary Monomer chromatin subunits prepared by micrococcal nuclease digestion showed a monophasic thermal denaturation transition with a Tm of about 77°C. By contrast, dimers and higher oligomers gave a biphasic melting profile, with Tms at 45–55°C and 77°C.
C L, Woodcock, L L, Frado
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Reversible thermal denaturation of Aplysia myoglobin

Journal of Molecular Biology, 1968
Abstract Ferric Aplysia myoglobin undergoes a rapidly reversible thermal denaturation in the range of 55 to 70 °C. In salt-free solution the high-temperature form precipitates, while in the presence of salts (ionic strength approx. 0.1 or higher) it remains soluble. The thermal transition, as studied in salt solution, is associated with large changes
M, Brunori, E, Antonini, P, Fasella, J, Wyman, A R, Fanelli   +4 more
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CALORIMETRIC INVESTIGATION OF RIBONUCLEASE THERMAL DENATURATION

International Journal of Peptide and Protein Research, 1973
Thermal denaturation of ribonuclease has been investigated by scanning microcalorimetric, spectrophotometric and polarimetric techniques. It is shown that the temperature changes of ribonuclease are of a complicated character and may be subdivided by the temperature region into two qualitatively different stages: (a) the predenaturational stage, at ...
P L, Privalov, E I, Tiktopulo, N N, Khechinashvili   +2 more
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Thermal Denaturation Profiles of Tuna Myoglobin

Bioscience, Biotechnology, and Biochemistry, 2010
Myoglobin (Mb) purified from fast skeletal muscle of bluefin tuna Thunnus thynnus orientalis was subjected to thermal treatment, and the denaturation profiles were examined by thermodynamic analysis. Based on the ellipticity or helical content obtained by circular dichroism (CD) spectrometry, it was found that denaturation of tuna Mb consisted of three
Yoshihiro, Ochiai, Yoshiaki, Watanabe, Hideo, Ozawa, Shigeru, Ikegami, Naoyuki, Uchida, Shugo, Watabe   +5 more
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