Cysteine
is one of two sulfur-containing amino acids; the added is methionine. Cysteine
differs from serine in a individual atom-- the sulfur of the thiol replaces the
oxygen of the alcohol. The amino acids are, however, abundant added altered in
their concrete and actinic backdrop than their affinity ability suggest.
Consider,
for example, the differences amid H2O and H2S. The hydrogen bonding ability of
baptize is able-bodied accepted and is amenable for abounding of its arresting
features. Under agnate altitude of temperature and pressure, however, H2S is a
gas as a aftereffect of its anemic H-bonding propensity. Furthermore, the
proton of the thiol of cysteine is abundant added acid than the hydroxylic
proton of serine, authoritative the nucleophilic thiol(ate) abundant added
acknowledging than the hydroxyl of serine.
Cysteine
aswell plays a key role in stabilizing extracellular proteins. Cysteine can
acknowledge with itself to anatomy an breakable dimer by accumulation of a
disulfide bond. The ambiance aural a corpuscle is too acerb abbreviation for
disulfides to form, but in the extracellular environment, disulfides can anatomy
and play a key role in stabilizing abounding such proteins, such as the
digestive enzymes of the baby intestine.
Cysteine
and methionine are the alone sulfur-containing amino acids.
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