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R is the gas constant and T is the absolute temperature. Note that pK a = −log(K a) and 2.303 ≈ ln(10). At 25 °C, ΔG ⊖ in kJ·mol −1 ≈ 5.708 pK a (1 kJ·mol −1 = 1000 joules per mole). Free energy is made up of an enthalpy term and an entropy term. [11] =
The conjugate base of glyoxylic acid is known as glyoxylate and is the form that the compound exists in solution at neutral pH. Glyoxylate is the byproduct of the amidation process in biosynthesis of several amidated peptides.
In computational biology, protein pK a calculations are used to estimate the pK a values of amino acids as they exist within proteins.These calculations complement the pK a values reported for amino acids in their free state, and are used frequently within the fields of molecular modeling, structural bioinformatics, and computational biology.
In cell biology, protein kinase A (PKA) is a family of serine-threonine kinase [1] whose activity is dependent on cellular levels of cyclic AMP (cAMP). PKA is also known as cAMP-dependent protein kinase (EC 2.7.11.11). PKA has several functions in the cell, including regulation of glycogen, sugar, and lipid metabolism.
In its path, a PKA can produce effects similar to those of heating and rapidly quenching a metal, resulting in Frenkel defects. A thermal spike does not last long enough to permit annealing of the Frenkel defects. [1] [2] A different model called the displacement spike was proposed for fast neutron bombardment of heavy elements.
The pKa's occur in two distinct ranges because deprotonations occur on separate phosphate groups. For comparison with the p K a 's for phosphoric acid are 2.14, 7.20, and 12.37. At physiological pH 's, pyrophosphate exists as a mixture of doubly and singly protonated forms.
The pKa of KHP is 5.4, so its pH buffering range would be 4.4 to 6.4; however, due to the presence of the second acidic group that bears the potassium ion, the first pKa also contributes to the buffering range well below pH 4.0, which is why KHP is a good choice for use as a reference standard for pH 4.00. [8] [9]
Inactive PKA exists as a tetramer consisting of a regulatory (R) subunit dimer and two catalytic (C) subunits. This PKA holoenzyme complex is tethered to cell membranes and organelles through association with A-kinase-anchoring proteins (AKAPs). The addition of cAMP causes a conformational change in the anchored R subunits that releases the C ...