Abstract
Capping of both N- and C-terminal induce α-helix formation in Cu2+-His6 peptide.
Highlights
An ensemble of structures of metal-hexa-histidine-tag capped and uncapped peptides has been studied using molecular dynamics simulations
The typical (His)6-tag is linked to the C- or N-terminus of the protein, and it serves as a molecular ‘anchor’ that binds to a metal ion, immobilized by chelation with nitrilotriacetic acid (NTA) bound to a solid support
One can assume that the termini capping of the metal-binding His-tag will not affect its conformational structure; we suggest that the capping of the peptide termini signi cantly shi s the energy landscape of the metalpeptide complexes, affects its conformational structure and allows the stabilization of different conformations
Summary
An ensemble of structures of metal-hexa-histidine-tag capped and uncapped peptides has been studied using molecular dynamics simulations. The capping of the peptide termini promotes a-helical conformations that are induced by the metal binding sites. We further suggest that the capping of the peptide leads to population shi and to the conformational change of metal binding peptides.
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