Results 241 to 250 of about 116,006 (295)

Flexibility and thermal denaturation (melting) of irradiated DNA

, 1996
Loukakis, GK, Sideris, EG, Georgakilas, AG, Kalfas, CA, Anagnostopoulou-Konsta, A   +4 more
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An Optimized Staining Method for Visualization of Thermally Denatured Dermal Collagen. [PDF]

Lasers Surg Med
Ahn GR, Quadri SA, Downs HM, T Suwan P, Wang-Evers M, Warner-Levy J, Manstein D.   +6 more
europepmc   +1 more source

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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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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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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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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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Thermal denaturation of lobster hemocyanin

Biochimica et Biophysica Acta, 1957
Abstract 1. 1. A procedure for the determination of heat denaturation of hemocyanin by means of changes in specific refractive increment has been presented. The method possesses the advantage of requiring a small volume (0.1 ml) of solution for analysis. 2. 2.
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The effect of thermal denaturation on the antigenicity of glycinin

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971
Abstract The effect of temperature and time of heating on the antigenicity of glycinin was investigated by the methods of radial immunodiffusion, complement fixation, and disc immunoelectrophoresis. The protein retains its immunological activity by heating for 30 min even up to 65°. However, a rapid loss in antigenicity is observed in the temperature
N, Catsimpoolas, J, Kenney, E W, Meyer
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