Ontology highlight
ABSTRACT:
SUBMITTER: Takei T
PROVIDER: S-EPMC4420536 | biostudies-literature | 2015 May
REPOSITORIES: biostudies-literature
Takei Toshiaki T Tsumoto Kouhei K Okonogi Atsuhito A Kimura Akiko A Kojima Shuichi S Yazaki Kazumori K Takei Tsunetomo T Ueda Takuya T Miura Kin-ichiro K
Protein science : a publication of the Protein Society 20150402 5
We reported previously that our designed polypeptide α3 (21 residues), which has three repeats of a seven-amino-acid sequence (LETLAKA)3, forms not only an amphipathic α-helix structure but also long fibrous assemblies in aqueous solution. To address the relationship between the electrical states of the polypeptide and its α-helix and fibrous assembly formation, we characterized mutated polypeptides in which charged amino acid residues of α3 were replaced with Ser. We prepared the following poly ...[more]