A comparison of the alpha-helix forming propensities and hydrogen bonding properties of serine phosphate and alpha-amino-gamma-phosphonobutyric acid

Bioorg Med Chem Lett. 1999 Sep 20;9(18):2759-62. doi: 10.1016/s0960-894x(99)00469-2.

Abstract

The ability of serine phosphate (SerP) or alpha-amino-gamma-phosphonobutyric acid (AbuP) and arginine to form a salt bridge between their side chains appears to be much greater when they are spaced i/i+4 than when they are spaced i/i+3. The side chain-side chain interaction between SerP/Arg and AbuP/Arg, positioned i/i+4, contribute 0.45 and 0.62 kcal mol(-1), respectively, toward stabilizing the alpha-helical conformation of a peptide.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Aminobutyrates / chemistry*
  • Circular Dichroism
  • Hydrogen Bonding
  • Molecular Sequence Data
  • Peptides / chemistry
  • Phosphoserine / chemistry*
  • Protein Conformation

Substances

  • Aminobutyrates
  • Peptides
  • Phosphoserine
  • 2-amino-4-phosphonobutyric acid