ChemBioChem · 2010 · 37 citations · 18 references
Life SciencesBiochemistryMolecular BiologyProtein EngineeringProtein FoldingStructural BiologyProtein DesignProtein Folding PathwaysProtein MisfoldingProtein RefoldingProtein StructureSecondary Structure FormationAmino AcidsMutational EffectsMutational RobustnessNoncanonical Amino AcidsProtein FoldsProtein Sequence DesignResidue Incorporation EffectsRobustness
Folding up: Residue-specific incorporation of noncanonical amino acids (NCAAs) often results in loss of protein function either by misfolding or aggregation (left). However, engineering the protein sequence for enhanced folding increases the mutational robustness of the protein to accommodate novel side chains and generate tailor-made proteins with new properties (right). Detailed facts of importance to specialist readers are published as ”Supporting Information”. Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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The Neutral Theory of Molecular Evolution
Scientific American · 1979 · 7.8K citations
FACS-optimized mutants of the green fluorescent protein (GFP)
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Protein stability promotes evolvability
Jesse D. Bloom, Sy T. Labthavikul, Christopher R. Otey et al. · Proceedings of the National Academy of Sciences · 2006 · 1.3K citations · Full text