Abstract
Hydrated proteins and DNA demonstrate a dynamic transition at temperatures T D-200-230K. Sharp slowing down of protein functions (rate of biochemical reactions) was observed at the same temperature range. These results suggest a direct relationship between the dynamic transition and onset of biochemical activities of proteins. However, the microscopic nature of the dynamic transition in biomolecules remains poorly understood. This contribution presents an overview of neutron scattering and simulations data analyzing dynamics of proteins and DNA. We show that the dynamic transition is related to a "slow" relaxation process that appears in the experimental frequency window at temperatures above T D. Moreover, we show that the dynamic crossover in the solvents controls the activation of the slow process in biological macromolecules. Microscopic details of the slow process and of the dynamic transition are discussed.
| Original language | English |
|---|---|
| Article number | Q2.5 |
| Pages (from-to) | 41-50 |
| Number of pages | 10 |
| Journal | Materials Research Society Symposium Proceedings |
| Volume | 840 |
| State | Published - 2005 |
| Externally published | Yes |
| Event | Neutron and X-Ray Scattering as Probes of Multiscale Phenomena - Boston, MA, United States Duration: Nov 29 2004 → Dec 1 2004 |