Electrostatic determinants of stability in parallel 3-stranded coiled coils.
The optimal positioning of salt-bridging interactions in a parallel alpha-helical homotrimeric coiled coil has been explored in a metal ion-assembled polypeptide trimer of 60 residues; arginine-glutamate pairs are more stabilizing than the corresponding lysine-glutamate pairs, and optimal stabilization is obtained with positively charged arginine residues at the c positions of the alpha-helical heptad and negatively charged glutamate residues at the e positions.
Roy
Liton
L
Department of Chemistry, University of Vermont, Burlington, VT, USA.
Case
Martin A
MA
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D004151:Dipeptides / Q000737:chemistry; D005971:Glutamates / Q000737:chemistry; D007477:Ions; D008239:Lysine / Q000737:chemistry; D008670:Metals / Q000737:chemistry; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012492:Salts / Q000737:chemistry; D055672:Static Electricity; D014508:Urea / Q000737:chemistry
D004151:Dipeptides; D005971:Glutamates; D007477:Ions; D008670:Metals; D009842:Oligopeptides; D012492:Salts; D014508:Urea; D008239:Lysine; C024362:arginine glutamate