Association between foldability and aggregation propensity in small disulfide-rich proteins.

ABSTRACT:

Aims

Disulfide-rich domains (DRDs) are small proteins whose native structure is stabilized by the presence of covalent disulfide bonds. These domains are versatile and can perform a wide range of functions. Many of these domains readily unfold on disulfide bond reduction, suggesting that in the absence of covalent bonding they might display significant disorder.

Results

Here, we analyzed the degree of disorder in 97 domains representative of the different DRDs families and demonstrate that, in terms of sequence, many of them can be classified as intrinsically disordered proteins (IDPs) or contain predicted disordered regions. The analysis of the aggregation propensity of these domains indicates that, similar to IDPs, their sequences are more soluble and have less aggregating

SUBMITTER: Fraga H 

PROVIDER: S-EPMC4076991 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature