Hyperstable miniproteins: additive effects of D- and L-Ala mutations

Org Biomol Chem. 2008 Dec 7;6(23):4287-9. doi: 10.1039/b814314e. Epub 2008 Oct 15.

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.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Alanine / genetics*
  • Alanine / metabolism*
  • Amino Acid Sequence
  • Circular Dichroism
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Mutant Proteins / chemistry*
  • Mutant Proteins / genetics
  • Mutant Proteins / metabolism*
  • Mutation*
  • Peptides / chemistry
  • Peptides / genetics*
  • Peptides / metabolism*
  • Protein Denaturation
  • Stereoisomerism
  • Thermodynamics
  • Transition Temperature

Substances

  • Mutant Proteins
  • Peptides
  • Trp-cage peptide
  • Alanine