Predicting protein folding pathways at the mesoscopic level based on native interactions between secondary structure elements

Background: Since experimental determination of protein folding pathways remains difficult, computational techniques are often used to simulate protein folding. Most current techniques to predict protein folding pathways are computationally intensive and are suitable only for small proteins. Results: By assuming that the native structure of a protein is known and representing each intermediate conformation as a collection of fully folded structures in which each of them contains a set of interacting secondary structure elements, we show that it is possible to significantly reduce the conformation space while still being able to predict the most energetically favorable folding pathway of large proteins with hundreds of residues at the mesoscopic level, including the pig muscle phosphoglycerate kinase with 416 residues. The model is detailed enough to distinguish between different folding pathways of structurally very similar proteins, including the streptococcal protein G and the pepto...

• Type: Journal
• Year: 2008
• Where: BMCBI
• Authors: Qingwu Yang, Sing-Hoi Sze
• Keywords: BMCBI 2008, Folding Pathways, Protein, Small Proteins