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Conversely, when pH = pK a, the concentration of HA is equal to the concentration of A −. The buffer region extends over the approximate range pK a ± 2. Buffering is weak outside the range pK a ± 1. At pH ≤ pK a − 2 the substance is said to be fully protonated and at pH ≥ pK a + 2 it is fully dissociated (deprotonated).
The Henderson–Hasselbalch equation can be used to model these equilibria. It is important to maintain this pH of 7.4 to ensure enzymes are able to work optimally. [10] Life threatening Acidosis (a low blood pH resulting in nausea, headaches, and even coma, and convulsions) is due to a lack of functioning of enzymes at a low pH. [10]
The pH range is commonly given as zero to 14, but a pH value can be less than 0 for very concentrated strong acids or greater than 14 for very concentrated strong bases. [2] The pH scale is traceable to a set of standard solutions whose pH is established by international agreement. [3]
In a buffer, a weak acid and its conjugate base (in the form of a salt), or a weak base and its conjugate acid, are used in order to limit the pH change during a titration process. Buffers have both organic and non-organic chemical applications. For example, besides buffers being used in lab processes, human blood acts as a buffer to maintain pH.
The pH of tears shift throughout a waking day, rising "about 0.013 pH units/hour" until a prolonged closed-eye period causes the pH to fall again. [15] Most healthy individuals have tear pH in the range of 7.0 to 7.7, where bicarbonate buffering is the most significant, but proteins and other buffering components are also present that are ...
In and of themselves, pH indicators are usually weak acids or weak bases. The general reaction scheme of acidic pH indicators in aqueous solutions can be formulated as: HInd (aq) + H 2 O (l) ⇌ H 3 O + (aq) + Ind − (aq) where, "HInd" is the acidic form and "Ind −" is the conjugate base of the indicator. Vice versa for basic pH indicators ...
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Typically, the effects of the protein environment on the amino acid pK a value are divided into pH-independent effects and pH-dependent effects. The pH-independent effects (desolvation, interactions with permanent charges and dipoles) are added to the model pK a value to give the intrinsic pK a value. The pH-dependent effects cannot be added in ...