N-Terminal sequences of α-crystallin

Brdtain N - Terminal Sequences of a - Crystallin

The amino acid sequences at the N-terminal ends of the chains of the lens protein, a-crystallin, were studied. Both the main kinds of chain in bovine ix-crystallin (A chains and B chains) have an N-terininal methionine residue, and the amino group is acetylated. Selective purification of the peptides in a tryptic digest of bovirne a-crystallin gave a preparation consisting largely of the N-term...

2342 α-Crystallin: A micelle or N-mer aggregate?

w This work aims to test the hypothesis that age-related loss of the molecular chaperone activity of a-crystallin may be involved in the precipitation of lens proteins and subsequent cataract development. &&Q& acrystallins of dierent ages were isolated from concentric tissue layers removed from foetal and adull bovine lenses. They were examined for chaperone activity by measuring their ability ...

Structure/function studies of dogfish α-crystallin, comparison with bovine α-crystallin

PURPOSE alpha-Crystallin is the major protein of the mammalian lens where it contributes to the refractive properties needed for vision and possibly to the stability of the tissue. The aim of this study was to determine whether the properties of alpha-crystallin have changed during the course of evolution. METHODS Dogfish alpha-crystallin, which appeared over 420 million years ago, has been c...

Exploring the accessible conformations of N-terminal acetylated α-synuclein.

Alpha synuclein (αsyn) fibrils are found in the Lewy Bodies of patients with Parkinson's disease (PD). The aggregation of the αsyn monomer to soluble oligomers and insoluble fibril aggregates is believed to be one of the causes of PD. Recently, the view of the native state of αsyn as a monomeric ensemble was challenged by a report suggesting that αsyn exists in its native state as a helical tet...

Synthesis of lens protein in vitro. N-terminal acetylation of alpha-crystallin.