Fig. 7
From: Pushing the mass limit for intact launch and photoionization of large neutral biopolymers
Structural parameters obtained with canonical-ensemble molecular dynamics simulations. a Temperature dependence of the radius of gyration 〈RG〉 of polypeptide (6). Even when starting from a stretched state, the molecule rapidly coils into a closed tertiary structure with increasing temperature. b The average solvent accessible surface area 〈SASA〉 quantifies the exposure of different parts of the molecule, here to vacuum. The total area (blue squares) decreases with increasing temperature, as expected but slowly increases beyond 300 K because of the increased exposure of the fluoroalkyl chains (green circles). The tryptophan residues (magenta diamonds) remain almost fully exposed at all temperatures, while the lysine surface (orange triangles) shrinks slightly. Error bars correspond to the standard deviation of the mean.
