Large anhydrous polyalanine ions: evidence for extended helices and onset of a more compact state.
Ion mobility measurements and molecular modeling calculations have been used to examine the conformations of large multiply charged polyalanine peptides. Two series of [Ala(n)+3H](3+) conformations which do not interconvert during the 10 to 30 ms experimental timescales are observed: a family of elongated structures for n = 18 to 39 and a series of more compact conformations for n = 24 to 41. The more compact state becomes the dominant conformer type for n > 32. Molecular modeling studies and comparisons of calculated collision cross sections with experiment indicate that the elongated ions have extended helical conformations. We suggest that the more compact state corresponds to a new conformer type: a folded hinged helix-coil state in which helical and coil regions have similar physical dimensions. The competition between extended and compact states is rationalized by considering differences in charge stabilization and entropy.
Counterman
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AE
Department of Chemistry, Indiana University, Bloomington, Indiana 47405, USA.
Clemmer
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DE
D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary
D010455:Peptides; C019529:polyalanine