作者: Stefan Walter , Johannes Buchner
DOI: 10.1002/1521-3773(20020402)41:7<1098::AID-ANIE1098>3.0.CO;2-9
关键词: Structural biology 、 Cell biology 、 Co-chaperone 、 Chemistry 、 Protein structure 、 Protein design 、 Protein folding 、 Chaperone (protein) 、 Protein engineering 、 Chaperonin 、 Biochemistry 、 General chemistry 、 Catalysis
摘要: Proteins are linear polymers synthesized by ribosomes from activated amino acids. The product of this biosynthetic process is a polypeptide chain, which has to adopt the unique three-dimensional structure required for its function in cell. In 1972, Christian Anfinsen was awarded Nobel Prize Chemistry showing that folding autonomous it does not require any additional factors or input energy. Based on vitro experiments with purified proteins, suggested correct can form spontaneously vivo once newly protein leaves ribosome. Furthermore, proteins were assumed maintain their native conformation until they degraded specific enzymes. last decade view cellular changed considerably. It become clear complicated and sophisticated machinery exists assists allows functional state be maintained under conditions would normally unfold aggregate. These collectively called molecular chaperones, because, like human counterparts, prevent unwanted interactions between immature clients. review, we discuss principal features peculiar class ± relationships, underlying mechanisms.