ReviewProtein science : a publication of the Protein Society2004
De novo proteins from designed combinatorial libraries.
Review in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
65 citing papers in PubMed.
- Emergence and evolution of protein-coding de novo genes.Nature reviews. Genetics · 2026Review
- Science of the gaps.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Article
- Article
- Spiers Memorial Lecture: Engineering biocatalysts.Faraday discussions · 2024Article
- Sequence, Structure, and Functional Space of Drosophila De Novo Proteins.Genome biology and evolution · 2024Article
- Crystal structure and activity of a de novo enzyme, ferric enterobactin esterase Syn-F4.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Design and Selection of Heterodimerizing Helical Hairpins for Synthetic Biology.ACS synthetic biology · 2023Article
- A de novo protein catalyzes the synthesis of semiconductor quantum dots.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Self-Assembling Lectin Nano-Block Oligomers Enhance Binding Avidity to Glycans.International journal of molecular sciences · 2022Article
- De novo metalloprotein design.Nature reviews. Chemistry · 2022Article
- Rational thermostabilisation of four-helix bundle dimeric de novo proteins.Scientific reports · 2021Article
- The temperature dependence of amino acid hydrophobicity data is related to the genetic coding algorithm for complementary (sense and antisense) peptide interactions.Data in brief · 2020Article
- Review
- Unevolved De Novo Proteins Have Innate Tendencies to Bind Transition Metals.Life (Basel, Switzerland) · 2019Article
- A new era for understanding amyloid structures and disease.Nature reviews. Molecular cell biology · 2018Review
- The de novo design of a biocompatible and functional integral membrane protein using minimal sequence complexity.Scientific reports · 2018Article
- Designed for life: biocompatible de novo designed proteins and components.Journal of the Royal Society, Interface · 2018Review
- Hierarchical design of artificial proteins and complexes toward synthetic structural biology.Biophysical reviews · 2018Review
- Global analysis of protein folding using massively parallel design, synthesis, and testing.Science (New York, N.Y.) · 2017Article
- Fact or fiction: updates on how protein-coding genes might emergeF1000Research · 2017Review
5 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors.
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Abstract
Combinatorial libraries of de novo amino acid sequences can provide a rich source of diversity for the discovery of novel proteins with interesting and important activities. Randomly generated sequences, however, rarely fold into well-ordered proteinlike structures. To enhance the quality of a library, features of rational design must be used to focus sequence diversity into those regions of sequence space that are most likely to yield folded structures. This review describes how focused libraries can be constructed by designing the binary pattern of polar and nonpolar amino acids to favor proteins that contain abundant secondary structure, while simultaneously burying hydrophobic side chains and exposing hydrophilic side chains to solvent. The "binary code" for protein design was used to construct several libraries of de novo proteins, including both alpha-helical and beta-sheet structures. The recently determined solution structure of a binary patterned four-helix bundle is well ordered, thereby demonstrating that sequences that have neither been selected by evolution (in vivo or in vitro) nor designed by computer can form nativelike proteins. Examples are presented demonstrating how binary patterned libraries have successfully produced well-ordered structures, cofactor binding, catalytic activity, self-assembled monolayers, amyloid-like nanofibrils, and protein-based biomaterials.
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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.