Ia. Kaltashov et C. Fenselau, STABILITY OF SECONDARY STRUCTURAL ELEMENTS IN A SOLVENT-FREE ENVIRONMENT - THE ALPHA-HELIX, Proteins, 27(2), 1997, pp. 165-170
The stability of the or helix as an element of secondary structure is
examined in the absence of solvation, in the gas phase. Mass-analyzed
ion kinetic energy (MIKE) spectrometry was applied to measure intercha
rge repulsion and intercharge distance in multiply protonated melittin
, a polypeptide known to possess a stable helical structure in a numbe
r of different environments. The experimental results, interpreted in
combination with molecular mechanics calculations, suggest that triply
charged melittin retains its secondary structure in the gas phase, Th
e stability if the cu-helical conformation of the polypeptide in the a
bsence of solvent molecules reflects the fact that a network of intrin
sic helical hydrogen bonds is energetically more favorable than unfold
ed conformations. (C) 1997 Wiley-Liss, Inc.