Protein folding and deterministic chaos: Limits of protein folding simulations and calculations
✍ Scribed by Gerald Böhm
- Publisher
- Elsevier Science
- Year
- 1991
- Tongue
- English
- Weight
- 574 KB
- Volume
- 1
- Category
- Article
- ISSN
- 0960-0779
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract Topology‐based interaction potentials are simplified models that use the native contacts in the folded structure of a protein to define an energetically unfrustrated folding funnel. They have been widely used to analyze the folding transition and pathways of different proteins through c
We have performed 128 folding and 45 unfolding molecular dynamics runs of chymotrypsin inhibitor 2 (CI2) with an implicit solvation model for a total simulation time of 0.4 microseconds. Folding requires that the three-dimensional structure of the native state is known. It was simulated at 300 K by
The available experimental data on the kinetics of unfolding and refolding of small proteins are reviewed. Excluding slow transitions in the unfolded protein due to cis- trans isomerization of peptide bonds, the rate-limiting transition state in both unfolding and refolding is concluded to be a high