title: A surprising simplicity to protein folding.
abstract: The polypeptide chains that make up proteins have thousands of atoms and hence millions of possible inter-atomic interactions. It might be supposed that the resulting complexity would make prediction of protein structure and protein-folding mechanisms nearly impossible. But the fundamental physics underlying folding may be much simpler than this complexity would lead us to expect folding rates and mechanisms appear to be largely determined by the topology of the native (folded) state, and new methods have shown great promise in predicting protein-folding mechanisms and the three-dimensional structures of proteins.
authors.affiliation: Department of Biochemistry, University of Washington, Seattle 98195, USA.
authors.forename: D
authors.initials: D
authors.lastname: Baker
mesh_terms: D000595:Amino Acid Sequence; D008956:Models, Chemical; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding; D013816:Thermodynamics
chemical_list: D010455:Peptides