A Minimal Model for the Hydrophobic and Hydrogen Bonding Effects on Secondary and Tertiary Structure Formation in Proteins
A refinement of a minimal model for protein folding originally proposed by Imamura is presented. The representation of the alpha-helix has been improved by adding in explicit modelling of the entire peptide unit. A four-helix bundle consisting of four alpha-helices and three loop regions is generate...
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| Language: | en |
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2009
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| Online Access: | http://hdl.handle.net/10012/4370 |