TY - JOUR
T1 - Stabilization of α-helix structure by polar side-chain interactions
T2 - Complex salt bridges, cation-π interactions, and C-H···O H-bonds
AU - Shi, Zhengshuang
AU - Olson, C. Anders
AU - Bell, Anthony J.
AU - Kallenbach, Neville R.
PY - 2001
Y1 - 2001
N2 - 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-π, and C-H···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.
AB - 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-π, and C-H···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.
KW - C-H···O H-bonding interactions
KW - Cation-π interactions
KW - Complex salt bridge interactions
KW - Helical proteins
KW - Polar side-chain interactions
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U2 - 10.1002/1097-0282(2001)60:5<366::AID-BIP10177>3.0.CO;2-5
DO - 10.1002/1097-0282(2001)60:5<366::AID-BIP10177>3.0.CO;2-5
M3 - Review article
C2 - 12115147
AN - SCOPUS:0035746132
SN - 0006-3525
VL - 60
SP - 366
EP - 380
JO - Biopolymers - Peptide Science Section
JF - Biopolymers - Peptide Science Section
IS - 5
ER -