Ontology highlight
ABSTRACT:
SUBMITTER: Zhang Y
PROVIDER: S-EPMC4844985 | biostudies-literature | 2016 Apr
REPOSITORIES: biostudies-literature
Zhang Yuanzhao Y Weber Jeffrey K JK Zhou Ruhong R
Scientific reports 20160426
Though the problem of sequence-reversed protein folding is largely unexplored, one might speculate that reversed native protein sequences should be significantly more foldable than purely random heteropolymer sequences. In this article, we investigate how the reverse-sequences of native proteins might fold by examining a series of small proteins of increasing structural complexity (α-helix, β-hairpin, α-helix bundle, and α/β-protein). Employing a tandem protein structure prediction algorithmic a ...[more]