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
Cell dynamics of folding in two-dimensional model proteins
β Scribed by Marek Cieplak; Jayanth R Banavar
- Book ID
- 114382632
- Publisher
- Elsevier Science
- Year
- 1997
- Tongue
- English
- Weight
- 127 KB
- Volume
- 2
- Category
- Article
- ISSN
- 1359-0278
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## Abstract The noninteracting localβstructure model of the folding and unfolding transition in globular proteins, the formulation of which was given in the preceding paper, is applied to the analysis of the twoβdimensional lattice model of proteins. The lattice model of proteins is a theoretical t
## Abstract The cluster model of protein folding [Kanehisa, M. I. & Tsong, T. Y. (1978) __J. Mol. Biol.__ **124**, 177β194] is further investigated for the thermodynamic and kinetic properties of protein foldingβunfolding transitions. A cluster is a locally formed ordered region in the polypeptide