title: Hyperstable miniproteins: additive effects of D- and L-Ala mutations.
abstract: The folding enantioselectivity for D-Ala versus L-Ala at one glycine site in the Trp-cage is 16 kJ mol(-1); judicious introductions of alanines of the correct chirality raises the melting temperature of this 20-residue fold to 83 degrees C.
authors.affiliation: Department of Chemistry, University of Washington, Seattle, WA 98195, USA.
authors.forename: D Victoria
authors.initials: DV
authors.lastname: Williams
authors.forename: Bipasha
authors.initials: B
authors.lastname: Barua
authors.forename: Niels H
authors.initials: NH
authors.lastname: Andersen
mesh_terms: D000409:Alanine / Q000235:genetics* / Q000378:metabolism*; D000595:Amino Acid Sequence; D002942:Circular Dichroism; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D050505:Mutant Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D010455:Peptides / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D011489:Protein Denaturation; D013237:Stereoisomerism; D013816:Thermodynamics; D044366:Transition Temperature
chemical_list: D050505:Mutant Proteins; D010455:Peptides; C508725:Trp-cage peptide; D000409:Alanine