This study will present our attempts to extract information about structural transitions of single oligopeptides from measurements of their nanomechanical properties such as molecular stiffness and mechanical energy dissipation coefficients. For the case in question we will use a de novo synthetised 13 residue peptide with a helical propensity. First we performed a molecular dynamics (MD) study to characterize the populated structures and dynamical timescales corresponding to several experimental conditions. Second, we used single-molecule force-extension and force-clamp spectroscopies with AFM (SMFS-AFM) to obtain estimates of the mean structures available in folded and stretched states for the single peptide molecules immobilized on custom substrates. We analyzed the results to address the question whether the simulated structures and motions could be employed to provide microscopic interpretations for our nanomechanical measurements.

Investigations of structural and nanomechanical properties of a custom made oligopeptide with a helical propensity: MD and SMFS-AFM study

ACS Fall 2021

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