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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
Hideo Ozawa   +5 more
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Stochastic dynamics and denaturation of thermalized DNA

Physical Review E, 2008
In the first part of the paper, the stochastic dynamics of the Peyrard-Bishop-Dauxois (PBD) DNA model is studied. A one-dimensional averaged Itô stochastic differential equation governing the total energy of the system and the associated Fokker-Planck equation governing the transition probability density function of the total energy are derived from ...
Mao Lin Deng, Weiqiu Zhu, Weiqiu Zhu
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Impact of structural stability of cold adapted Candida antarctica lipase B (CaLB): in relation to pH, chemical and thermal denaturation

, 2015
The effect of pH on the conformational behavior of Candida antartica lipase B (CaLB) has been monitored by spectroscopic and calorimetric studies. The results obtained from far and near-UV CD, intrinsic fluorescence and ANS binding studies indicate that ...
G. Rabbani   +5 more
semanticscholar   +1 more source

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 ...
N.N. Khechinashvili   +2 more
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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
Paolo Fasella   +9 more
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Visualization of thermally denatured nucleosomes

Proceedings, annual meeting, Electron Microscopy Society of America, 1978
Electron 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.
V. L. Seligy, N. H. Poon
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Thermal denaturation of pea globulins (Pisum sativum L.)-molecular interactions leading to heat-induced protein aggregation.

Journal of Agricultural and Food Chemistry, 2013
The heat-induced denaturation and aggregation of mixed pea globulins (8%, w/w) were investigated using differential scanning calorimetry (DSC), SDS-PAGE, and size-exclusion chromatography (SEC-HPLC).
Jean-luc Mession   +3 more
semanticscholar   +1 more source

Antigenicity of thermal denatured yoshida glycoprotein

Experientia, 1976
The 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. Caputo, A. Floridi
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Vibrational circular dichroism spectra of lysozyme solutions: solvent effects on thermal denaturation processes.

Journal of Physical Chemistry B, 2013
Vibrational spectroscopy has been applied to the study of conformational variation of lysozyme during thermal denaturation. An infrared and vibrational circular dichroism (VCD) analysis of lysozyme in D2O, D2O/EtOD, and D2O/DMSO at different solvent ...
A. Giugliarelli   +5 more
semanticscholar   +1 more source

A SIMPLE MODEL FOR PROTEIN THERMAL DENATURATION*

International Journal of Peptide and Protein Research, 1978
Whether proteins denature in an all‐or‐none fashion or in a continuous fashion is as yet an unresolved problem. The all‐or‐none process implies that while the process of denaturation is going on, only two kinds of protein molecules can exist. One is completely unchanged and the other is altered.
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