Salt dependence of an alpha-helical peptide folding energy landscapes.
We used CD, UV resonance Raman spectroscopy, and molecular dynamics simulation to examine the impact of salts on the conformational equilibria and the Ramachandran Psi angle (un)folding Gibbs free energy landscape coordinate of a mainly polyalanine alpha-helical peptide, AP of sequence AAAAA(AAARA)(3)A. NaClO(4) stabilizes alpha-helical-like conformations more than does NaCl, which stabilizes more than Na(2)SO(4) at identical ionic strengths. This alpha-helix stabilization ordering is the reverse of the Hofmeister series of anions in their ability to disorder water hydrogen bonding. Much of the NaClO(4) alpha-helix stabilization results from ClO(4)(-) association with the AP terminal -NH(3)(+) groups and Arg side chains. ClO(4)(-) stabilizes 3(10)-helix conformations but destabilizes turn conformations. The decreased Cl(-) and SO(4)(2-) AP alpha-helix stabilization probably results from a decreased association with the Arg and terminal -NH(3)(+) groups. Cl(-) is expected to have a smaller binding affinity and thus stabilizes alpha-helical conformations intermediately between NaClO(4) and Na(2)SO(4). Electrostatic screening stabilizes pi-bulge conformations.
Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA.
Kan
K
Xiong
Eliana K
EK
Asciutto
Jeffry D
JD
Madura
Sanford A
SA
Asher
D006860:Hydrogen Bonding; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D012492:Salts / Q000737:chemistry*; D013057:Spectrum Analysis / Q000379:methods
D010455:Peptides; D012492:Salts