Exploring the dark foldable proteome by considering hydrophobic amino acids topology.

ABSTRACT: The protein universe corresponds to the set of all proteins found in all organisms. A way to explore it is by taking into account the domain content of the proteins. However, some part of sequences and many entire sequences remain un-annotated despite a converging number of domain families. The un-annotated part of the protein universe is referred to as the dark proteome and remains poorly characterized. In this study, we quantify the amount of foldable domains within the dark proteome by using the hydrophobic cluster analysis methodology. These un-annotated foldable domains were grouped using a combination of remote homology searches and domain annotations, leading to define different levels of darkness. The dark foldable domains were analyzed to understand what make them different from d

SUBMITTER: Bitard-Feildel T 

PROVIDER: S-EPMC5278394 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature