title: Protein folding in the post-genomic era.
abstract: Protein folding is a topic of fundamental interest since it concerns the mechanisms by which the genetic message is translated into the three-dimensional and functional structure of proteins. In these post-genomic times, the knowledge of the fundamental principles are required in the exploitation of the information contained in the increasing number of sequenced genomes. Protein folding also has practical applications in the understanding of different pathologies and the development of novel therapeutics to prevent diseases associated with protein misfolding and aggregation. Significant advances have been made ranging from the Anfinsen postulate to the "new view" which describes the folding process in terms of an energy landscape. These new insights arise from both theoretical and experimental studies. The problem of folding in the cellular environment is briefly discussed. The modern view of misfolding and aggregation processes that are involved in several pathologies such as prion and Alzheimer diseases. Several approaches of structure prediction, which is a very active field of research, are described.
authors.affiliation: Institut de Biochimie Biophysique Moléculaire et Cellulaire, UMR Centre National de la Recherche Scientifique, Université de Paris-Sud, Orsay, France. jeannine.yon@mip.u-psud.fr
authors.forename: Jeannine M
authors.initials: JM
authors.lastname: Yon
mesh_terms: D000686:Amyloidosis / Q000378:metabolism / Q000473:pathology; D000818:Animals; D018834:Chaperonin 60 / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D010735:Phosphoglycerate Kinase / Q000737:chemistry; D011328:Prions / Q000737:chemistry / Q000378:metabolism; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D018834:Chaperonin 60; D011328:Prions; D010735:Phosphoglycerate Kinase