Hyperstable miniproteins: additive effects of D- and L-Ala mutations.
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.
Williams
D Victoria
DV
Department of Chemistry, University of Washington, Seattle, WA 98195, USA.
Barua
Bipasha
B
Andersen
Niels H
NH
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
D050505:Mutant Proteins; D010455:Peptides; C508725:Trp-cage peptide; D000409:Alanine