An evolution of minimalist models for protein folding: from the behavior of protein-like polymers to protein function
β Scribed by John Karanicolas; Charles L. Brooks III
- Book ID
- 117803056
- Publisher
- Elsevier Science
- Year
- 2004
- Tongue
- English
- Weight
- 251 KB
- Volume
- 2
- Category
- Article
- ISSN
- 1741-8364
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
The partition function of the two-dimensional lattice HP model for protein folding is computed by exact enumeration. For a protein-like sequence, the distribution of partiton function zeros shows roughly a two-ring pattern, while for a nonprotein-like sequence, the outer ring of zeros is ill-develop
## Abstract In this study, freeβenergy function (FEF) for discriminating the native fold of a protein from misfolded decoys was investigated. It is a physicsβbased function using an allβatom model, which comprises the hydration entropy (HE) and the total dehydration penalty (TDP). The HE is calcula