Folding funnels and frustration in off-lattice minimalist protein landscapes
AUTOR(ES)
Nymeyer, Hugh
FONTE
The National Academy of Sciences
RESUMO
A full quantitative understanding of the protein folding problem is now becoming possible with the help of the energy landscape theory and the protein folding funnel concept. Good folding sequences have a landscape that resembles a rough funnel where the energy bias towards the native state is larger than its ruggedness. Such a landscape leads not only to fast folding and stable native conformations but, more importantly, to sequences that are robust to variations in the protein environment and to sequence mutations. In this paper, an off-lattice model of sequences that fold into a β-barrel native structure is used to describe a framework that can quantitatively distinguish good and bad folders. The two sequences analyzed have the same native structure, but one of them is minimally frustrated whereas the other one exhibits a high degree of frustration.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=34496Documentos Relacionados
- Strategies for optimize off-lattice aggregate simulations
- Structure optimization of the two-dimensional off-lattice hydrophobic–hydrophilic model
- A minimalist model protein with multiple folding funnels
- Energy-based de novo protein folding by conformational space annealing and an off-lattice united-residue force field: Application to the 10-55 fragment of staphylococcal protein A and to apo calbindin D9K
- Balancing energy and entropy: A minimalist model for the characterization of protein folding landscapes