Results 221 to 230 of about 105,310 (260)

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, Wei Qiu, Zhu
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Monitoring protein denaturation using thermal conductivity probe

International Journal of Biological Macromolecules, 2013
We propose a method for probing denaturation of proteins by measuring the thermal conductivity of the solution. We use the three-omega method with a microfabricated ac thermal sensor to measure the thermal conductivity of lysozyme, β-lactoglobulin, and bovine serum albumin protein solutions over a range of temperature and pH.
Byoung kyoo Park, Namwoo Yi, Park, J, Kim, D   +3 more
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Kinetics of thermal denaturation of antithrombin III

Biotechnology and Bioengineering, 1982
AbstractPurified 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).
G, Mitra, P M, Schneider, J L, Lundblad
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Dissociative mechanism of F-actin thermal denaturation

Biochemistry (Moscow), 2006
We have applied differential scanning calorimetry to investigate thermal unfolding of F-actin. It has been shown that the thermal stability of F-actin strongly depends on ADP concentration. The transition temperature, T(m), increases with increasing ADP concentration up to 1 mM.
V V, Mikhailova, B I, Kurganov, A V, Pivovarova, D I, Levitsky   +3 more
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Effects of thermal denaturation on protein glycation

Life Sciences, 2002
Protein denaturation occurs at sites of inflammation. We hypothesized that denatured protein may provide a more susceptible target for glycation, which is a known mediator of inflammation. We examined the effects of thermal denaturation on the susceptibility of protein glycation using glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and aspartate ...
Norbert W, Seidler, George S, Yeargans
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Thymus deoxyribonucleoprotein I. Preparation and thermal denaturation

Biochimica et Biophysica Acta, 1962
Abstract Preparations of undissociated deoxyribonucleoprotein having a reproducible composition were obtained from calf-thymus glands essentially by extraction with water. Spectrophotometric titration and other ultraviolet-absorption measurements showed that this deoxyribonucleoprotein was denatured by heat and by alkali in both 0.001 M and 1.0 M
K, MURRAY, A R, PEACOCKE
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The thermal denaturation of chromatin core particles

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
The thermal denaturation of chicken erythrocyte core particles has been followed using changes in absorption and circular dichroism. The absorption-denaturation curve is biphasic, with transitions centred at 59 degrees C and 74 degrees C. The first of these transitions is reversible, whereas heating into the second transition produces irreversible ...
I O, Walker, A P, Wolffe
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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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Thermal denaturation of alpha-crystallin.

Lens and eye toxicity research, 1991
Low molecular weight alpha-crystallin, isolated from cow lenses, exhibit irreversible thermal denaturation in solution at 75 degrees C. The heat of denaturation was obtained from a differential scanning calorimetric endothermic peak. A second run on the denatured alpha-crystallin solution showed that the denaturation is irreversible.
J A, Castoro, F A, Bettelheim
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Studies on the thermal denaturation of nucleohistones

Journal of Molecular Biology, 1973
Abstract The thermal denaturation profiles of nucleohistone from calf thymus, sea urchin sperm and sea cucumber male gonad, are studied and compared under a variety of conditions. These include melting in the presence of either one of the following agents: urea, methanol, divalent cations or excess histones.
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