Chaperonins are known to facilitate the productive folding of numerous misfolded proteins. Despite their established importance, the mechanism of chaperonin-assisted protein folding remains unknown. In the present article, all-atom explicit solvent molecular dynamics (MD) simulations have been perfo
Microsecond Explicit Solvent Molecular Dynamics Simulations of Protein Folding
β Scribed by Freddolino, Peter L.; Liu, Feng; Park, Sanghyun; Gruebele, Martin; Schulten, Klaus
- Book ID
- 122192083
- Publisher
- Biophysical Society
- Year
- 2009
- Tongue
- English
- Weight
- 59 KB
- Volume
- 96
- Category
- Article
- ISSN
- 0006-3495
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## Abstract A mixed Monte Carlo/Molecular Dynamics method using the trial moves for peptide backbone sampling known as Concerted Rotations with Angles was implemented. The algorithm was used to study polyalanine systems. Equivalent results to conventional Molecular Dynamics were obtained for simula
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