ArticleJournal of the American Chemical Society2010
De novo design and molecular assembly of a transmembrane diporphyrin-binding protein complex.
Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 118 citations in OpenAlex.
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- Understanding, inhibiting, and engineering membrane transporters with high-throughput mutational screens.Cell chemical biology · 2025Review
- Article
- Computational design of de novo bioenergetic membrane proteins.Biochemical Society transactions · 2024Review
- Next generation of multispecific antibody engineering.Antibody therapeutics · 2024Review
- Intelligent Protein Design and Molecular Characterization Techniques: A Comprehensive Review.Molecules (Basel, Switzerland) · 2023Review
- Cellular production of a de novo membrane cytochrome.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- Corrole-protein interactions in H-NOX and HasA.RSC chemical biology · 2022Article
- Supramolecular assembly of protein building blocks: from folding to function.Nano convergence · 2022Review
- Protein-protein interaction prediction with deep learning: A comprehensive review.Computational and structural biotechnology journal · 2022Review
- Dawn of a New Era for Membrane Protein Design.Biodesign research · 2022Review
- Protein-Embedded Metalloporphyrin Arrays Templated by Circularly Permuted Tobacco Mosaic Virus Coat Proteins.ACS nano · 2021Article
- Characteristics and therapeutic applications of antimicrobial peptides.Biophysics reviews · 2021Review
- Membrane Protein Engineering with Rosetta.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Small-residue packing motifs modulate the structure and function of a minimal de novo membrane protein.Scientific reports · 2020Article
- Semi-Rationally Designed Short Peptides Self-Assemble and Bind Hemin to Promote Cyclopropanation.Angewandte Chemie (International ed. in English) · 2020Article
- Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
The de novo design of membrane proteins remains difficult despite recent advances in understanding the factors that drive membrane protein folding and association. We have designed a membrane protein PRIME (PoRphyrins In MEmbrane) that positions two non-natural iron diphenylporphyrins (Fe(III)DPP's) sufficiently close to provide a multicentered pathway for transmembrane electron transfer. Computational methods previously used for the design of multiporphyrin water-soluble helical proteins were extended to this membrane target. Four helices were arranged in a D(2)-symmetrical bundle to bind two Fe(II/III) diphenylporphyrins in a bis-His geometry further stabilized by second-shell hydrogen bonds. UV-vis absorbance, CD spectroscopy, analytical ultracentrifugation, redox potentiometry, and EPR demonstrate that PRIME binds the cofactor with high affinity and specificity in the expected geometry.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.