Origins of the high 14-helix propensity of cyclohexyl-rigidified residues in beta-peptides.
[structure: see text] beta-Peptides containing residues derived from trans-2-aminocyclohexanecarboxylic acid (ACHC) display high population of 14-helical secondary structure in aqueous solution. We show that hydrophobic interactions between cyclohexyl rings are not responsible for this conformation-promoting effect, and that polar groups may be attached to the cyclohexyl ring without diminishing the effect.
Lee
Myung-Ryul
MR
Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
Raguse
Tami L
TL
Schinnerl
Marina
M
Pomerantz
William C
WC
Wang
Xiaodong
X
Wipf
Peter
P
Gellman
Samuel H
SH
D002942:Circular Dichroism; D003500:Cyclization; D009682:Magnetic Resonance Spectroscopy; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary
D010455:Peptides