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Synthetic Foldable Proteins Generated from Peptide Segments of Folding Nuclei of Reference Proteins
Experimental support for the foldability-function tradeoff hypothesis
Prebiotic Protein Design supports a Halophile Origin of Foldable Proteins
Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein.
Ab initio Folding of a Trefoil-fold Motif Reveals Structural similarity with a β-propeller Blade Motif
Evolution and design of protein structure by folding nucleus symmetric expansion
Mutation Choice to Eliminate Buried Free Cysteines in Protein Therapeutics
Simplified Protein Design Biased for Pre-Biotic Amino Acids Yields a Foldable, Halophilic Protein
Characterization of binding of LARP6 to the 5' stem-loop of collagen mRNAs
Emergence of Symmetric Protein Architecture from a Simple Peptide Motif
Alternative Folding Nuclei Definitions Facilitate the Evolution of a Symmetric Protein Fold from a Smaller Peptide Motif
Folding Nucleus Structure Persists in Thermally-Aggregated FGF-1
Kallikrein-related Peptidase 6
Evolution of a Protein Folding Nucleus
Single Aromatic Core Mutation Converts a Designed "Primitive" Protein from Halophile to Mesophile Folding
Symmetry and Simplicity in Protein Evolution and Design