Results 331 to 340 of about 2,723,431 (383)
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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 ...
B. Liljesvan +2 more
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Effect of diethylsulfoxide on the thermal denaturation of DNA
Biopolymers, 2006AbstractDNA thermal denaturation has been investigated in aqueous solutions of diethylsulfoxide (DESO) by means of UV‐vis and densimetry methods. It is suggested that, on the one hand, the structural change of entire solutions and, on the other hand, a direct interaction of DESO with DNA are responsible for the observed peculiar behavior.
Hasmik R. Sargsyan +3 more
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Effects of thermal denaturation on binding between bixin and whey protein.
Journal of Agricultural and Food Chemistry, 2012Heating is commonly used in the manufacture of dairy products, but impacts of thermal denaturation on binding between whey protein and molecules such as pigments are poorly understood.
Yue Zhang, Q. Zhong
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Kinetics of thermal denaturation of antithrombin III
Biotechnology and Bioengineering, 1982AbstractPurified antithrombin III (AT III), a single‐chain human plasma glycoprotein, molecular weight 58,000 daltons, and one of the major serine protease inhibitors, was heated in the 60–70°C range for inactivating possible contaminations by hepatitis B virus (HBV).
J. L. Lundblad +2 more
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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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Journal of Physical Chemistry B, 2011
Biopreservation by saccharides is a widely studied issue due to its scientific and technological importance; in particular, ternary amorphous protein-saccharide-water systems are extensively exploited to model the characteristics of the in vivo ...
G. Bellavia +4 more
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Biopreservation by saccharides is a widely studied issue due to its scientific and technological importance; in particular, ternary amorphous protein-saccharide-water systems are extensively exploited to model the characteristics of the in vivo ...
G. Bellavia +4 more
semanticscholar +1 more source
The thermal denaturation of nucleoprotein in boar sperm
Journal of Molecular Biology, 1965The paper describes a study of the thermal denaturation of DNA in intact boar sperm. A recently designed microspectrophotometer was used to measure the integrated absorption at 260 m μ of sperm after they had been heated in several media. Denaturation was detected with heating media containing 70% glycerol and 30% of a sodium chloride-sodium citrate ...
Peter J. Chamberlain, Peter M.B. Walker
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[33] Thermal denaturation procedures for hemoglobin
1994Publisher Summary The stability of cross-linked hemoglobins is an important aspect in evaluating them as potential blood substitutes. Both of these situations require a quantitative measurement of hemoglobin stability that can be used to compare different species.
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Effects of thermal denaturation on the solid-state structure and molecular mobility of glycinin.
Biomacromolecules, 2011The effects of moisture and thermal denaturation on the solid-state structure and molecular mobility of soy glycinin powder were investigated using multiple techniques that probe over a range of length and time scales.
M. Huson +7 more
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The effect of thermal denaturation on the antigenicity of glycinin
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971Abstract 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
J. A. Kenney +2 more
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