A comparison of the alpha-helix forming propensities and hydrogen bonding properties of serine phosphate and alpha-amino-gamma-phosphonobutyric acid.
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.
Liehr
S
S
Department of Chemistry and Biochemistry, University of Delaware, Newark 19711, USA.
Chenault
H K
HK
D000595:Amino Acid Sequence; D000613:Aminobutyrates / Q000737:chemistry*; D002942:Circular Dichroism; D006860:Hydrogen Bonding; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D010768:Phosphoserine / Q000737:chemistry*; D011487:Protein Conformation
D000613:Aminobutyrates; D010455:Peptides; D010768:Phosphoserine; C012729:2-amino-4-phosphonobutyric acid