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Using multicanonical simulations, the authors study the effect of charged endgroups on helix formation in alanine based polypeptides. They confirm earlierreports that neutral polyalanine exhibits a pronounced helix-coil transition ingas phase simulations. Introducing a charged Lys+ at the C terminal stabilizesthe helix and leads to a higher transition temperature. On the other hand,adding the Lys+ at the N terminal inhibits helix formation. Instead, a moreglobular structure was found. These results are in agreement with recentexperiments on alanine based polypeptides in gas phase. They indicate thatpresent force fields describe accurately the intramolecular interactions inproteins.

On the Helix-coil Transition in Alanine-based Polypeptides in Gas Phase