Elucidating the folding problem of helical peptides using empirical parameters.
Using an empirical analysis of experimental data we have estimated a set of energy contributions which accounts for the stability of isolated alpha-helices. With this database and an algorithm based on statistical mechanics, we describe the average helical behaviour in solution of 323 peptides and the helicity per residue of those peptides analyzed by nuclear magnetic resonance. Moreover the algorithm successfully detects the alpha-helical tendency, in solution, of a peptide corresponding to a beta-strand of ubiquitin.
Muñoz
V
V
EMBL, Heidelberg, Germany.
Serrano
L
L
D000465:Algorithms; D000595:Amino Acid Sequence; D002942:Circular Dichroism; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012996:Solutions; D014452:Ubiquitins / Q000737:chemistry
D012996:Solutions; D014452:Ubiquitins