title: Conformations of co-translational folding intermediates.
abstract: While in vitro experiments have contributed much to our understanding of protein folding, we know much less about how proteins fold in the more complex environment of the cell. This review summarizes our current knowledge of the earliest in vivo folding intermediates: the conformations adopted by nascent polypeptides during synthesis by the ribosome. The challenges related to successful folding in the cellular environment, including off-pathway aggregation and macromolecular crowding, are also discussed.
authors.affiliation: Department of Chemistry and Biochemistry, University of Notre Dame, 251 Nieuwland Science Hall, Notre Dame, IN 46556, USA.
authors.forename: Michael S
authors.initials: MS
authors.lastname: Evans
authors.forename: Thomas F
authors.initials: TF
authors.lastname: Clarke
authors.forename: Patricia L
authors.initials: PL
authors.lastname: Clark
mesh_terms: D005057:Eukaryotic Cells / Q000502:physiology; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D011387:Prokaryotic Cells / Q000502:physiology; D014176:Protein Biosynthesis; D011487:Protein Conformation; D017510:Protein Folding; D012270:Ribosomes / Q000378:metabolism
chemical_list: D010455:Peptides