ArticleScientific reports2018
The de novo design of a biocompatible and functional integral membrane protein using minimal sequence complexity.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 22 citations in OpenAlex.
- Computational design of de novo bioenergetic membrane proteins.Biochemical Society transactions · 2024Review
- Cellular production of a de novo membrane cytochrome.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Dissecting the stability determinants of a challenging de novo protein fold using massively parallel design and experimentation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- Small-residue packing motifs modulate the structure and function of a minimal de novo membrane protein.Scientific reports · 2020Article
- Designing minimalist membrane proteins.Biochemical Society transactions · 2019Review
Corrections and comments
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Authors and funding
14 authors at 1 institution in 1 country.
Funding
Abstract
The de novo design of integral membrane proteins remains a major challenge in protein chemistry. Here, we describe the bottom-up design of a genetically-encoded synthetic membrane protein comprising only four amino acids (L, S, G and W) in the transmembrane domains. This artificial sequence, which we call REAMP for recombinantly expressed artificial membrane protein, is a single chain of 133 residues arranged into four antiparallel membrane-spanning α-helices. REAMP was overexpressed in Escherichia coli and localized to the cytoplasmic membrane with the intended transmembrane topology. Recombinant REAMP could be extracted from the cell membrane in detergent micelles and was robust and stable in vitro, containing helical secondary structure consistent with the original design. Engineered mono- and bis-histidine residues in the membrane domain of REAMP were able to coordinate heme in vitro, in a manner reminiscent of natural b-type cytochromes. This binding shifted the electrochemical potential of the cofactor, producing a synthetic hemoprotein capable of nascent redox catalysis. These results show that a highly reduced set of amino acids is sufficient to mimic some key properties of natural proteins, and that cellular biosynthesis is a viable route for the production of minimal de novo membrane sequences.
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Registered trials
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