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Nucleic acid thermodynamics is the study of how temperature affects the nucleic acid structure of double-stranded DNA (dsDNA). The melting temperature (T m) is defined as the temperature at which half of the DNA strands are in the random coil or single-stranded (ssDNA) state.
Crystal structure of β-glucosidase from Thermotoga neapolitana (PDB: 5IDI).Thermostable protein, active at 80°C and with unfolding temperature of 101°C. [1]In materials science and molecular biology, thermostability is the ability of a substance to resist irreversible change in its chemical or physical structure, often by resisting decomposition or polymerization, at a high relative ...
In thermodynamics, the thermodynamic free energy is one of the state functions of a thermodynamic system.The change in the free energy is the maximum amount of work that the system can perform in a process at constant temperature, and its sign indicates whether the process is thermodynamically favorable or forbidden.
An even number of protons or neutrons is more stable (higher binding energy) because of pairing effects, so even–even nuclides are much more stable than odd–odd. One effect is that there are few stable odd–odd nuclides: in fact only five are stable, with another four having half-lives longer than a billion years.
Fluorescence in situ hybridization (FISH) is a laboratory method used to detect and locate a DNA sequence, often on a particular chromosome. [4]In the 1960s, researchers Joseph Gall and Mary Lou Pardue found that molecular hybridization could be used to identify the position of DNA sequences in situ (i.e., in their natural positions within a chromosome).
In thermodynamics, thermal stability describes the stability of a water body and its resistance to mixing. [1] It is the amount of work needed to transform the water to a uniform water density . The Schmidt stability "S" is commonly measured in joules per square meter (J/m 2 ).
A thermal shift assay (TSA) measures changes in the thermal denaturation temperature and hence stability of a protein under varying conditions such as variations in drug concentration, buffer formulation (pH or ionic strength), redox potential, or sequence mutation. The most common method for measuring protein thermal shifts is differential ...
Polyacrylamide gel electrophoresis (PAGE) is a technique widely used in biochemistry, forensic chemistry, genetics, molecular biology and biotechnology to separate biological macromolecules, usually proteins or nucleic acids, according to their electrophoretic mobility. Electrophoretic mobility is a function of the length, conformation, and ...