ArticleJournal of molecular biology2016
De Novo Proteins with Life-Sustaining Functions Are Structurally Dynamic.
Article in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Review
- An expandable, modular de novo protein platform for precision redox engineering.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Protein-protein interaction prediction with deep learning: A comprehensive review.Computational and structural biotechnology journal · 2022Review
- A Strategy for Combinatorial Cavity Design in De Novo Proteins.Life (Basel, Switzerland) · 2020Article
- A de novo peroxidase is also a promiscuous yet stereoselective carbene transferase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Protein ensembles link genotype to phenotype.PLoS computational biology · 2019Review
- The de novo design of a biocompatible and functional integral membrane protein using minimal sequence complexity.Scientific reports · 2018Article
- The ascent of man(made oxidoreductases).Current opinion in structural biology · 2018Review
- A de novo enzyme catalyzes a life-sustaining reaction in Escherichia coli.Nature chemical biology · 2018Article
- Random protein sequences can form defined secondary structures and are well-tolerated in vivo.Scientific reports · 2017Article
- Foldamer hypothesis for the growth and sequence differentiation of prebiotic polymers.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme.Nature communications · 2017Article
- Flexible Proteins at the Origin of Life.Life (Basel, Switzerland) · 2017Article
- The coming of age of de novo protein design.Nature · 2016Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Designing and producing novel proteins that fold into stable structures and provide essential biological functions are key goals in synthetic biology. In initial steps toward achieving these goals, we constructed a combinatorial library of de novo proteins designed to fold into 4-helix bundles. As described previously, screening this library for sequences that function in vivo to rescue conditionally lethal mutants of Escherichia coli (auxotrophs) yielded several de novo sequences, termed SynRescue proteins, which rescued four different E. coli auxotrophs. In an effort to understand the structural requirements necessary for auxotroph rescue, we investigated the biophysical properties of the SynRescue proteins, using both computational and experimental approaches. Results from circular dichroism, size-exclusion chromatography, and NMR demonstrate that the SynRescue proteins are α-helical and relatively stable. Surprisingly, however, they do not form well-ordered structures. Instead, they form dynamic structures that fluctuate between monomeric and dimeric states. These findings show that a well-ordered structure is not a prerequisite for life-sustaining functions, and suggests that dynamic structures may have been important in the early evolution of protein function.
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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.