Relevance of structural segregation and chain compaction for the thermodynamics of folding of a hydrophobic protein model
Author:
Publisher
American Physical Society (APS)
Link
http://harvest.aps.org/v2/journals/articles/10.1103/PhysRevE.67.051919/fulltext
Reference20 articles.
1. Folding protein models with a simple hydrophobic energy function: The fundamental importance of monomer inside/outside segregation
2. Sequence rotation in N-dimensional space and the folding of hydrophobic protein models: Surpassing the diagonal unfolded state approximation
3. Folding simulations of a three-dimensional protein model with a nonspecific hydrophobic energy function
4. Non-native interactions, effective contact order, and protein folding: A mutational investigation with the energetically frustrated hydrophobic model
5. Emergence of Preferred Structures in a Simple Model of Protein Folding
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4. Alternative hydrogen bond implementations produce opposite effects on collapse cooperativity of lattice homopolypeptide models;Physical Review E;2007-11-20
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