Results 201 to 210 of about 105,310 (260)

Stress-Induced Antibody Aggregates: Insights from Native SEC-MS with Postcolumn Denaturation. [PDF]

open access: yesJ Am Soc Mass Spectrom
Ivanov D   +9 more
europepmc   +1 more source

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
openaire   +3 more sources

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   +3 more
openaire   +2 more sources

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   +3 more
openaire   +2 more sources

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
openaire   +2 more sources

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   +4 more
openaire   +2 more sources

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