page_title: Chaperone (protein)
hierarchical_section_title: Chaperone (protein)
caption_attribution_description: A top-view of the GroES/GroEL protein complex. Image created using Rasmol.
context_page_description: In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding and the assembly or disassembly of other macromolecular structures. Chaperones are present when the macromolecules perform their normal biological functions and have correctly completed the processes of folding and/or assembly. The chaperones are concerned primarily with protein folding. The first protein to be called a chaperone assists the assembly of nucleosomes from folded histones and DNA and such assembly chaperones, especially in the nucleus, are concerned with the assembly of folded subunits into oligomeric structures.
  One major function of chaperones is to prevent both newly synthesised polypeptide chains and assembled subunits from aggregating into nonfunctional structures. It is for this reason that many chaperones, but by no means all, are heat shock proteins because the tendency to aggregate increases as proteins are denatured by stress. In this case, chaperones do not convey any additional steric information required for proteins to fold.
context_section_description: In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding and the assembly or disassembly of other macromolecular structures. Chaperones are present when the macromolecules perform their normal biological functions and have correctly completed the processes of folding and/or assembly. The chaperones are concerned primarily with protein folding. The first protein to be called a chaperone assists the assembly of nucleosomes from folded histones and DNA and such assembly chaperones, especially in the nucleus, are concerned with the assembly of folded subunits into oligomeric structures.
  One major function of chaperones is to prevent both newly synthesised polypeptide chains and assembled subunits from aggregating into nonfunctional structures. It is for this reason that many chaperones, but by no means all, are heat shock proteins because the tendency to aggregate increases as proteins are denatured by stress. In this case, chaperones do not convey any additional steric information required for proteins to fold. However, some highly specific 'steric chaperones' do convey unique structural (steric) information onto proteins, which cannot be folded spontaneously. Such proteins violate Anfinsen's dogma, requiring protein dynamics to fold correctly.
  Various approaches have been applied to study the structure, dynamics and functioning of chaperones. Bulk biochemical measurements have informed us on the protein folding efficiency, and prevention of aggregation when chaperones are present during protein folding. Recent advances in single-molecule analysis have brought insights into structural heterogeneity of chaperones, folding intermediates and affinity of chaperones for unstructured and structured protein chains.
caption: A top-view of the GroES/GroEL bacterial chaperone complex model
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