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Stability of secondary structural elements in a solvent-free environment: the α helix

✍ Scribed by Igor A. Kaltashov; Catherine Fenselau

Publisher
John Wiley and Sons
Year
1997
Tongue
English
Weight
108 KB
Volume
27
Category
Article
ISSN
0887-3585

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✦ Synopsis

The stability of the a 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 intercharge repulsion and intercharge distance in multiply protonated melittin, a polypeptide known to possess a stable helical structure in a number 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. The stability if the a-helical conformation of the polypeptide in the absence of solvent molecules reflects the fact that a network of intrinsic helical hydrogen bonds is energetically more favorable than unfolded conformations. Proteins 27:165-170

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