ArticleBiochemical Society transactions2008
Controlling complexity and water penetration in functional de novo protein design.
Article in Biochemical Society transactions, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed.
- Article
- Protein dynamics govern the oxyferrous state lifetime of an artificial oxygen transport protein.Biophysical journal · 2023Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- Fast, cheap and out of control--Insights into thermodynamic and informatic constraints on natural protein sequences from de novo protein design.Biochimica et biophysica acta · 2016Article
- Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.Chemical Society reviews · 2015Review
- Elementary tetrahelical protein design for diverse oxidoreductase functions.Nature chemical biology · 2013Article
- Designing functional metalloproteins: from structural to catalytic metal sites.Coordination chemistry reviews · 2013Article
- Dynamic factors affecting gaseous ligand binding in an artificial oxygen transport protein.Biochemistry · 2013Article
- Engineering oxidoreductases: maquette proteins designed from scratch.Biochemical Society transactions · 2012Review
- Manipulating cofactor binding thermodynamics in an artificial oxygen transport protein.Biochemistry · 2011Article
- Designing artificial enzymes by intuition and computation.Nature chemistry · 2010Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Natural proteins are complex, and the engineering elements that support function and catalysis are obscure. Simplified synthetic protein scaffolds offer a means to avoid such complexity, learn the underlying principles behind the assembly of function and render the modular assembly of enzymatic function a tangible reality. A key feature of such protein design is the control and exclusion of water access to the protein core to provide the low-dielectric environment that enables enzymatic function. Recent successes in de novo protein design have illustrated how such control can be incorporated into the design process and have paved the way for the synthesis of nascent enzymatic activity in these systems.
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Registered trials
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