Results 211 to 220 of about 105,310 (260)
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CALORIMETRIC INVESTIGATION OF RIBONUCLEASE THERMAL DENATURATION
International Journal of Peptide and Protein Research, 1973Thermal 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 +2 more
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Thermal Denaturation Profiles of Tuna Myoglobin
Bioscience, Biotechnology, and Biochemistry, 2010Myoglobin (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 +5 more
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Antigenicity of thermal denatured yoshida glycoprotein
Experientia, 1976The correlation between antigenic functionality and conformation of Yoshida glycoprotein upon heating has been investigated. Heating modifies the conformation of the antigen, but does not abolish the reaction with its specific antibody.
A, Floridi, A, Caputo
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High-resolution analyzer of thermal denaturation
Analytical Biochemistry, 1974Abstract Details are given for the construction of a high-resolution denaturation analyzer for nucleic acid-containing macromolecules. The system contains the following new components: Peltier elements, guided by a linear resistance thermometer for temperature control, electronic microstirrer for quick thermal equilibration within the sample cell ...
P, Näslund +2 more
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Thermal Denaturation Assays in Chemical Biology
ASSAY and Drug Development Technologies, 2012Thermal denaturation-based methods are becoming increasingly used to characterize protein stability and interactions. Recent technical advances have made these methods more suitable for high throughput screening. Reasonable throughput and the ability to perform these screens using commonly used instruments, such as RT-PCR machines or simple plate ...
Guillermo, Senisterra +2 more
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Thermal denaturation of lobster hemocyanin
Biochimica et Biophysica Acta, 1957Abstract 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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Thermal Fluctuations in Histone During Denaturation
Journal of Nanoscience and Nanotechnology, 2007In 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
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Ligand-induced biphasic thermal denaturation of RNAase A
Journal of Thermal Analysis, 1994DSC measurements have been accomplished in aqueous solutions of bovine pancreatic ribonuclease A (RNAase A) in the presence of subsaturating amounts of 3′ cytidine monophosphate (3′ CMP) and 2′ cytidine monophosphate (2′ CMP) atpH 5.0 and 5.5. In these conditions the experimental profiles do not conform to a one-step unfolding process.
G. BARONE +5 more
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Thermal denaturation of collagen revisited
Proceedings / Indian Academy of Sciences, 1999We have recently re-examined the characteristic sharp denaturation temperature of the collagen molecule and fibre. It has been generally accepted for many years that denaturation is an equilibrium process involving the rupture of hydrogen bonds. We have now proposed that the process is an irreversible rate process, in which uncoupling of thea-chains ...
Christopher A Miles, Allen J Bailey
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Visualization of thermally denatured nucleosomes
Proceedings, annual meeting, Electron Microscopy Society of America, 1978Electron images of biological specimens composed of periodic structures are generally spurious. The reason is that unit structures may superimpose along the direction of view, and a “see through” image is formed especially from negatively stained and unstained objects.
N. H. Poon, V. L. Seligy
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