Designed multi-stranded heme binding β-sheet peptides in membrane.

ABSTRACT: Designed peptides demonstrating well-defined structures and functioning in membrane environment are of significant interest in developing novel proteins for membrane active biological processes including enzymes, electron transfer, ion channels and energy conversion. Heme proteins' ability to carry out multiple functions in nature has inspired the design of several helical heme binding peptides and proteins soluble in water and also recently in membrane. Naturally occurring β-sheet proteins are both water and membrane soluble, and are known to bind heme, however, designed heme binding β-sheet proteins are yet to be reported, plausibly because of the complex folding and difficulty in introducing heme binding sites in the β-sheet structures. Here, we describe the design, NMR structures and b

SUBMITTER: D'Souza A 

PROVIDER: S-EPMC5477022 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature