Estimation of interatomic free energies and protein folding
β Scribed by X. De la Cruz; J. Reverte; I. Fita
- Publisher
- Elsevier Science
- Year
- 1991
- Tongue
- English
- Weight
- 136 KB
- Volume
- 9
- Category
- Article
- ISSN
- 0263-7855
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π SIMILAR VOLUMES
Many seemingly unrelated protein families share common folds. Theoretical models based on structure designability have suggested that a few folds should be very common while many others have low probability. In agreement with the predictions of these models, we show that the distribution of observed
## 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
We have calculated the free energy of a spherical model of a protein or part of a protein generated in the way of protein folding. Two spherical models are examined; one is a homogeneous model consisting of only one residue type-hydrophobic. The other is a heterogeneous model consisting of two resid