enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  2. Equilibrium unfolding - Wikipedia

    en.wikipedia.org/wiki/Equilibrium_unfolding

    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.

  3. Enoyl CoA isomerase - Wikipedia

    en.wikipedia.org/wiki/Enoyl_CoA_isomerase

    In that sense, for many higher organisms, the mitochondrial enzyme is essential for deriving maximum energy from lipids and fueling muscles. [9] If the enzyme is unclear, react it with an enoyl CoA Derivative. If the enzyme gives off more than one product, it is a multifunctional enzyme. If it gives off one product, it is solely enoyl Co-Al ...

  4. GC-content - Wikipedia

    en.wikipedia.org/wiki/GC-content

    In molecular biology and genetics, GC-content (or guanine-cytosine content) is the percentage of nitrogenous bases in a DNA or RNA molecule that are either guanine (G) or cytosine (C). [1] This measure indicates the proportion of G and C bases out of an implied four total bases, also including adenine and thymine in DNA and adenine and uracil ...

  5. Glycolysis - Wikipedia

    en.wikipedia.org/wiki/Glycolysis

    The change in free energy, ΔG, for each step in the glycolysis pathway can be calculated using ΔG = ΔG°′ + RTln Q, where Q is the reaction quotient. This requires knowing the concentrations of the metabolites. All of these values are available for erythrocytes, with the exception of the concentrations of NAD + and NADH.

  6. Transition state theory - Wikipedia

    en.wikipedia.org/wiki/Transition_state_theory

    Using the Eyring equation, there is a straightforward relationship between ΔG ‡, first-order rate constants, and reaction half-life at a given temperature. At 298 K, a reaction with ΔG ‡ = 23 kcal/mol has a rate constant of k ≈ 8.4 × 10 −5 s −1 and a half life of t 1/2 ≈ 2.3 hours, figures that are often rounded to k ~ 10 −4 s ...

  7. Denaturation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Denaturation_(biochemistry)

    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]

  8. Glucose-6-phosphate isomerase - Wikipedia

    en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase

    The large domain, located at the N-terminal, and the C-terminal of each monomer also contain "arm-like" protrusions. [8] [9] Several residues in the small domain serve to bind phosphate, while other residues, particularly His 388, from the large and C-terminal domains are crucial to the sugar ring-opening step catalyzed by this enzyme. Since ...

  9. Fatty acid desaturase - Wikipedia

    en.wikipedia.org/wiki/Fatty_acid_desaturase

    This enzyme is responsible for the conversion of saturated fatty acids to unsaturated fatty acids in the synthesis of vegetable oils. Cyanobacterial DesA, [19] an enzyme that can introduce a second cis double bond at the delta-12 position of fatty acid bound to membrane glycerolipids. This enzyme is involved in chilling tolerance; the phase ...