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Thermal Fluctuations in Histone During Denaturation [PDF]

open access: yesJournal of Nanoscience and Nanotechnology, 2007
In this paper, we address the issue of thermal fluctuations during the thermal denaturation of linker histone H1 which is the basic ingredient of chromatin assembly. We measure the thermal fluctuations using a sensitive nanocalorimeter based thermal fluctuation measurement set up which can measure fluctuations of the order of 1 part per billion.
Nagapriya, KS   +2 more
openaire   +3 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

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

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