Large proteins have a great tendency to aggregate but a low propensity to form amyloid fibrils.

ABSTRACT: The assembly of soluble proteins into ordered fibrillar aggregates with cross-β structure is an essential event of many human diseases. The polypeptides undergoing aggregation are generally small in size. To explore if the small size is a primary determinant for the formation of amyloids under pathological conditions we have created two databases of proteins, forming amyloid-related and non-amyloid deposits in human diseases, respectively. The size distributions of the two protein populations are well separated, with the systems forming non-amyloid deposits appearing significantly larger. We have then investigated the propensity of the 486-residue hexokinase-B from Saccharomyces cerevisiae (YHKB) to form amyloid-like fibrils in vitro. This size is intermediate between the size distribution

SUBMITTER: Ramshini H 

PROVIDER: S-EPMC3020945 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature