title: A coarse-grained approach to protein design: learning from design to understand folding.
abstract: Computational studies have given a great contribution in building our current understanding of the complex behavior of protein molecules; nevertheless, a complete characterization of their free energy landscape still represents a major challenge. Here, we introduce a new coarse-grained approach that allows for an extensive sampling of the conformational space of a large number of sequences. We explicitly discuss its application in protein design, and by studying four representative proteins, we show that the method generates sequences with a relatively smooth free energy surface directed towards the target structures.
authors: Department of Physics, University of Vienna, Vienna, Austria. ivan.coluzza@univie.ac.at
authors: Ivan
authors: I
authors: Coluzza
mesh_terms: D030562:Databases, Protein; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D015202:Protein Engineering / Q000379:methods*; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000235:genetics*; D012997:Solvents / Q000737:chemistry; D013816:Thermodynamics
chemical_list: D010455:Peptides; D011506:Proteins; D012997:Solvents