Search results
Results from the WOW.Com Content Network
In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]
A plot illustrating the dependence on temperature of the rates of chemical reactions and various biological processes, for several different Q 10 temperature coefficients. The rate ratio at a temperature increase of 10 degrees (marked by points) is equal to the Q 10 coefficient.
Different states within this ensemble may be associated with different aspects of an enzyme's function. For example, different conformations of the enzyme dihydrofolate reductase are associated with the substrate binding, catalysis, cofactor release, and product release steps of the catalytic cycle, [53] consistent with catalytic resonance theory.
Enzyme inhibitors are molecules that reduce or abolish enzyme activity, while enzyme activators are molecules that increase the catalytic rate of enzymes. These interactions can be either reversible (i.e., removal of the inhibitor restores enzyme activity) or irreversible (i.e., the inhibitor permanently inactivates the enzyme).
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. T m depends on the length of the DNA molecule and its specific ...
However, different restriction enzymes generates different ends, and the base composition of the ends produced by these enzymes may also differ, the melting temperature and therefore the optimal temperature can vary widely depending on the restriction enzymes used, and the optimum temperature for ligation may be between 4-15 ° C depending on ...
A large number of different methods of measuring the concentrations of substrates and products exist and many enzymes can be assayed in several different ways. Biochemists usually study enzyme-catalysed reactions using four types of experiments: [3] Initial rate experiments. When an enzyme is mixed with a large excess of the substrate, the ...
Further addition of substrate would not increase the rate, and the enzyme is said to be saturated. The Michaelis constant is not affected by the concentration or purity of an enzyme. [16] Its value depends both on the identity of the enzyme and that of the substrate, as well as conditions such as temperature and pH.