Synthetic biology applications would benefit from protein modules of reduced complexity that function orthogonally to cellular components. As many subcellular processes depend on peptide-protein or protein-protein interactions, designed polypeptides that can bring together other proteins controllably are particularly useful. Thanks to established sequence-to-structure relationships, helical bundles provide good starting points for such designs.
View Article and Find Full Text PDFpeptides and proteins that switch state in response to chemical and physical cues would advance protein design and synthetic biology. Here we report two designed systems that disassemble and reassemble upon site-specific phosphorylation and dephosphorylation, respectively. As starting points, we use hyperthermostable antiparallel and parallel coiled-coil heterotetramers, , AB systems, to afford control in downstream applications.
View Article and Find Full Text PDFPublication-associated plain language summaries are brief, jargon-free summaries of scientific publications. They are intended for a broad, non-expert audience to help maximize the accessibility of the publication. Plain language summaries are typically found alongside peer-reviewed publications or in supplementary materials and can be indexed in PubMed.
View Article and Find Full Text PDF-designed protein domains are increasingly being applied in biotechnology, cell biology, and synthetic biology. Therefore, it is imperative that these proteins be robust to superficial changes; i.e.
View Article and Find Full Text PDFProtein-protein interactions control a wide variety of natural biological processes. α-Helical coiled coils frequently mediate such protein-protein interactions. Due to the relative simplicity of their sequences and structures and the ease with which properties such as strength and specificity of interaction can be controlled, coiled coils can be designed to deliver a variety of non-natural protein-protein interaction domains.
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