Alpha crystallin: Difference between revisions

== Function ==

Alpha crystallin is known to be one of the primary structural proteins of the eye's lens, specifically crystallin types alpha (α), beta (β), and gamma (γ). While all types have essential roles in the eye, alpha-crystallin and its subunits make up 40% of the lens's protein composition. These crystallin proteins create stability in the lens and have the ability to impact an individual's vision because they provide lens transparency. In order to retain their eye's transparency in the absence of protein turnover, or the replacing and reproduction of proteins within a cell as the proteins become broken down, the protein must retain some form of longevity. Its longevity is generally assumed to be correlated with the long-term retention of its native structure. Its ability to maintain the structure for a prolonged period of time is related to the N-terminal residue as this terminal is correlated with protein life. Even though the N-terminal does impact protein longevity, it does not determine a protein's half-life completely. In alpha-crystallin, the N-terminus contains approximately 60 residues, some of which include isoleucine and alanine.