Stabilization of alpha-helix structure by polar side-chain interactions: complex salt bridges, cation-pi interactions, and C-H em leader O H-bonds.
It is generally understood that helical proteins are stabilized by a combination of hydrophobic and packing interactions, together with H-bonds and electrostatic interactions. Here we show that polar side-chain interactions on the surface can play an important role in helix formation and stability. We review studies on model helical peptides that reveal the effect of weak interactions between side chains on helix stability, focusing on some nonclassical side-chain-side-chain interactions: complex salt bridges, cation-pi, and C-H em leader O H-bonding interactions. Each of these can be shown to contribute to helix stability, and thus must be included in a comprehensive catalogue of helix stabilizing effects. The issue of the structure of the unfolded states of helical peptides is also discussed, in the light of recent experiments showing that these contain substantial amounts of polyproline II conformation.
Department of Chemistry, New York University, NY 10003, USA.
Z
Z
Shi
C A
CA
Olson
A J
AJ
Bell
N R
NR
Kallenbach
D000595:Amino Acid Sequence; D002412:Cations; D006859:Hydrogen / Q000737:chemistry; D006860:Hydrogen Bonding; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012492:Salts / Q000737:chemistry*; D013997:Time Factors
D002412:Cations; D010455:Peptides; D012492:Salts; C011083:polyproline; D006859:Hydrogen