Lattice models of protein folding permitting disordered native states
Journal of Chemical Physics, ISSN: 0021-9606, Vol: 116, Issue: 5, Page: 2261-2268
2002
- 8Citations
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Article Description
An overview is given on a study carried out to illustrate that a broad survey over possible energetic models, all sequences, and all conformations for short chains reveals curious disagreement among different cooperativity measures and purported governing factors, apparently due to permitting conformational flexibility in the native state. Globular native conformations are not the rule, and over a substantial range of energy functions, the favored native states for the most thermally stable and cooperatively folding sequences are high entropy ensembles of conformations having little consistent structure.
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