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Cristiano L Dias

Publications and source records attributed to Cristiano L Dias.

3 recordsLinked to original sources

Rupture of an extended object: a many-body Kramers calculation.

We show how an extended object's strain field is redistributed when the material ruptures under by thermal activation. Through analytical calculations and molecular dynamics simulations, we show that in a polymer chain the distribution is exponentially localized around the point of rupture. The length scale of localization is determined by the strain and microscopic parameters of the interaction potential. We also derive an analytic expression for the rate of bond rupture by consistently treating the collective modes of the chain and the effect of dissipation on those modes. Our theoretical estimates are of the same order of magnitude as those obtained by simulations, as compared to earlier theories which had overestimated the rate of rupture by approximately two orders of magnitude. It is also noteworthy that the correction comes about through the effective attempt frequency rather than the effective barrier height.

Journal Article↗

Designable structures are easy to unfold.

We study the structural stability of models of proteins for which the selected folds are unusually stable to mutation, that is, designable. A two-dimensional hydrophobic-polar lattice model was used to determine designable folds and these folds were investigated through Langevin dynamics. We find that the phase diagram of these proteins depends on their designability. In particular, highly designable folds are found to be weaker, i.e., easier to unfold, than low designable ones. We expect this to be related to protein flexibility.

Amino Acid Sequence↗

Scaling in force spectroscopy of macromolecules.

We use molecular dynamics to determine the force needed to rupture a chain molecule being stretched at constant loading rate and temperature. When all energy bonds of the molecule are identical, we find that the force F depends on the pulling rate r and temperature T according to F approximately const- T(1/3)|ln (r/T)|(1/3). When a single weak bond is introduced, this result is modified to F approximately const - T(2/3|ln (r/T)(2/3)|. This scaling, which is model independent, can be used with experiment to quantitatively extract relevant microscopic parameters.

Animals↗