Synthesis and physical properties of protein core mimetics.
A series of mimetic cores composed of a synthetic scaffold and amino acids have been constructed and their properties investigated in chloroform. A relative measure of H-bond strength was obtained by comparing temperature coefficients derived from variable-temperature (1)H NMR experiments. Although most templates had a strong H-bond, only a single template composed of D- and L-phenylalanines was able to form two strong H-bonds. Templates containing D- and L-leucines formed only a single H-bond. The results of these studies suggest that aromatic edge-to-face interactions provide greater stabilization energy than aliphatic-aromatic interactions in the tightly packed hydrophobic cores of proteins. Partial structures of the templates were derived by analyzing a series of two-dimensional (1)H NMR spectra and performing molecular mechanics calculations using AMBER and MMFF94 force fields.
Turk
J A
JA
Department of Chemistry, University of Cincinnati, Cincinnati, Ohio 45221-0172, USA.
Smithrud
D B
DB
D000596:Amino Acids / Q000737:chemistry; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D018716:Molecular Mimicry; D011487:Protein Conformation; D011506:Proteins / Q000138:chemical synthesis* / Q000737:chemistry*; D013698:Templates, Genetic
D000596:Amino Acids; D011506:Proteins