Role of electrostatic and van der Waals interactions on the in vacuo unfolding dynamics of lysozyme ions

The unfolding of protein ions in gas phase (or a vacuum) proceeds rapidly once the total charge reaches a critical value q ∗ . The actual q ∗ value depends on temperature, protein composition, and force field parameters. Here, using molecular dynamics simulations, we explore the onset of the unfoldi...

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Bibliographic Details
Published in:Chemical physics letters 2001-12, Vol.350 (3), p.277-285
Main Authors: Arteca, Gustavo A., Reimann, C.T., Tapia, O.
Format: Article
Language:English
Subjects:
Biological and medical sciences
Conformational dynamics in molecular biology
Dynamics and conformational changes
Fundamental and applied biological sciences. Psychology
Molecular biophysics
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Summary:The unfolding of protein ions in gas phase (or a vacuum) proceeds rapidly once the total charge reaches a critical value q ∗ . The actual q ∗ value depends on temperature, protein composition, and force field parameters. Here, using molecular dynamics simulations, we explore the onset of the unfolding transition at q>q ∗ and its dependence on the nonbonded interaction between monomers. Using lysozyme, we show that, although a loss of attractive cohesion reduces the critical charge for unfolding, the mechanism for the transition may remain essentially unchanged over a range of Coulombic and van der Waals interactions.
ISSN:0009-2614
1873-4448
DOI:10.1016/S0009-2614(01)01291-X