The formation of stable highly organized protein aggegrates, known as amyloid fibrils, is associated with several debilitating human diseases, including Alzheimer's disease, Parkinson's disease, and Creutzfeldt-Jakob disease. In each of these conditions, a peptide or protein that is normally soluble accumulates into insoluble fibrils. Muscle acylphosphatase (ACYP2) has emerged as a significant model system to study protein misfolding and aggregation. It is particularly suitable for these studies because muscle acylphosphatase is a small, simple protein of only 98 amino acids consisting of a five-stranded antiparallel β-sheet and two parallel α-helices. Mutations in ACYP2 between residues 16-31 and 87-98, which includes its phosphate binding site at Arg 23, significantly increases the rate of aggregation. These mutations correlate with changes in the hydrophobicity of ACYP2 and a conversion of the α-helical structures to β-sheets. Therefore, a reduction in the net charge of a protein may be a key determinant in some forms of protein deposition diseases.
Informations pour la commande
Nom du produit | Ref. Catalogue | COND. | Prix HT | QTÉ | Favoris | |
Anticorps ACYP2 (2B4) | sc-134247 | 100 µg/ml | $333.00 |