Converging concepts of protein folding in vitro and in vivo.
Most proteins must fold into precise three-dimensional conformations to fulfill their biological functions. Here we review recent concepts emerging from studies of protein folding in vitro and in vivo, with a focus on how proteins navigate the complex folding energy landscape inside cells with the aid of molecular chaperones. Understanding these reactions is also of considerable medical relevance, as the aggregation of misfolding proteins that escape the cellular quality-control machinery underlies a range of debilitating diseases, including many age-onset neurodegenerative disorders.
Hartl
F Ulrich
FU
Max Planck Institute of Biochemistry, Department of Cellular Biochemistry, Martinsried, Germany. uhartl@biochem.mpg.de
Hayer-Hartl
Manajit
M
D000818:Animals; D018835:Chaperonin 10 / Q000737:chemistry / Q000378:metabolism; D018834:Chaperonin 60 / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008954:Models, Biological; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism
D018835:Chaperonin 10; D018834:Chaperonin 60; D018832:Molecular Chaperones; D011506:Proteins