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Biological thermodynamics (Thermodynamics of biological systems) is a science that explains the nature and general laws of thermodynamic processes occurring in living organisms as nonequilibrium thermodynamic systems that convert the energy of the Sun and food into other types of energy.
Steady-states can be stable or unstable. A steady-state is unstable if a small perturbation in one or more of the concentrations results in the system diverging from its state. In contrast, if a steady-state is stable, any perturbation will relax back to the original steady state. Further details can be found on the page Stability theory.
Anfinsen's dogma, also known as the thermodynamic hypothesis, is a postulate in molecular biology. It states that, at least for a small globular protein in its standard physiological environment, the native structure is determined only by the protein's amino acid sequence . [ 1 ]
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 the less extensive technique of equilibrium unfolding, the fractions of folded and unfolded molecules (denoted as and , respectively) are measured as the solution conditions are gradually changed from those favoring the native state to those favoring the unfolded state, e.g., by adding a denaturant such as guanidinium hydrochloride or urea.
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.
Another characteristic common to nearly all self-assembled systems is their thermodynamic stability. For self-assembly to take place without intervention of external forces, the process must lead to a lower Gibbs free energy, thus self-assembled structures are thermodynamically more stable than the single, unassembled components. A direct ...
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 ...