Journal article
Protein Folding with Implicit Crowders: A Study of Conformational States Using the Wang-Landau Method
The journal of physical chemistry. B, v 115(9), pp 2006-2013
10 Mar 2011
PMID: 21319755
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
In this paper we introduce the idea of the implicit crowding method to study the statistical mechanical behaviors of folding of beta-sheet peptides. Using a simple bead-lattice model, we are able to consider, separately, the conformational entropy involving the bond angles along the backbone and the orientational entropy associated with the dihedral angles. We use a Ising-like model to partially account for the dihedral angle entropy and, implicitly, the hydrogen-bond formations. We also compare our results to recent experiments and find good quantitative agreement on the predicted folded fraction. On the basis of the predictions from the scaled particle theory, we investigate changes in the melting temperature of the protein, suggesting crowding enhanced stability for a variant of trpzip hairpin and a slight instability for the larger beta-sheet designed proteins.
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Details
- Title
- Protein Folding with Implicit Crowders: A Study of Conformational States Using the Wang-Landau Method
- Creators
- Travis Hoppe - Drexel UniversityJian-Min Yuan - Drexel University
- Publication Details
- The journal of physical chemistry. B, v 115(9), pp 2006-2013
- Publisher
- American Chemical Society; Washington, DC
- Number of pages
- 8
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Physics
- Web of Science ID
- WOS:000287833000011
- Scopus ID
- 2-s2.0-79952270887
- Other Identifier
- 991019168123004721
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- Web of Science research areas
- Chemistry, Physical