The Role of Molecular Chaperones Hsp70 And Hsp60 in Protein Folding

作者: Franz Ulrich Hartl

DOI: 10.1007/978-3-642-60929-9_17

关键词: Protein foldingChaperoninCo-chaperoneFoldaseCell biologyChemical chaperoneChemistryEndoplasmic reticulumChaperone (protein)Peptide sequence

摘要: Protein folding is a problem of fundamental biological importance. It has been known for more than three decades that all the information required acqisition native state contained in linear amino acid sequence polypeptide chain. Proteins can fold spontaneously vitro, at least under carefully chosen conditions, and this led to view also within cells newly–synthesized polypeptides reach their an essentially spontaneous reaction. Only very recently it realized not case. Cells contain complex machinery proteins, catalysts molecular chaperones, which mediate cytosol as well subcellular compartments such mitochondria, chloroplasts endoplasmic reticulum (Hartl et al., 1992). Molecular mostly constitutively expressed stress play preeminent role these processes.

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