Enumeration and comprehensive in-silico modeling of three-helix bundle structures composed of typical αα-hairpins.

ABSTRACT:

Background

The design of protein structures from scratch requires special attention to the combination of the types and lengths of the secondary structures and the loops required to build highly designable backbone structure models. However, it is difficult to predict the combinations that result in globular and protein-like conformations without simulations. In this study, we used single-chain three-helix bundles as simple models of protein tertiary structures and sought to thoroughly investigate the conditions required to construct them, starting from the identification of the typical αα-hairpin motifs.

Results

First, by statistical analysis of naturally occurring protein structures, we identified three αα-hairpins motifs that were specifically related to the left- and rig

SUBMITTER: Sakuma K 

PROVIDER: S-EPMC8474748 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature