{"doi":"10.1002/9780470015902.a0005721.pub2","title":"Protein Folding and Chaperones","abstract":"<jats:title>Abstract</jats:title>\n          <jats:sec>\n            <jats:label/>\n            <jats:p>\n              Proteins fold via specific pathways to achieve their native structure. Protein structures are, however, inherently unstable; hence folding and unfolding are in equilibrium. Protein instability is a major concern inside the cell. Specialised proteins called molecular chaperones are, therefore, required to assist proteins in folding and to prevent aggregation of folding intermediates. Many different classes of chaperones exist that are conserved throughout all kingdoms of life, many of which are known as heat‐shock proteins. Chaperones typically recognise hydrophobic patches, but the exact functions and mechanisms of action of the various chaperone classes are very different. The main chaperone classes\n              <jats:named-content content-type=\"biological-name\">Hsp70</jats:named-content>\n              ,\n              <jats:named-content content-type=\"biological-name\">Hsp90</jats:named-content>\n              ,\n              <jats:named-content content-type=\"biological-name\">Hsp100</jats:named-content>\n              and\n              <jats:named-content content-type=\"biological-name\">chaperonins</jats:named-content>\n              all depend on\n              <jats:named-content content-type=\"biological-name\">adenosine triphosphatase</jats:named-content>\n              (\n              <jats:named-content content-type=\"biological-name\">ATPase</jats:named-content>\n              ) cycles, which enable subtle activity control by co‐chaperones. The molecular understanding of the mechanism of both chaperones and protein folding are key problems in today's life sciences. The importance is illustrated by the fact that many diseases are associated with these processes.\n            </jats:p>\n          </jats:sec>\n          <jats:sec>\n            <jats:title>Key Concepts:</jats:title>\n            <jats:p>\n              <jats:list list-type=\"bullet\">\n                <jats:list-item>\n                  <jats:p>Proteins fold via pathways.</jats:p>\n                </jats:list-item>\n                <jats:list-item>\n                  <jats:p>Protein structures are labile.</jats:p>\n                </jats:list-item>\n                <jats:list-item>\n                  <jats:p>\n                    Protein folding\n                    <jats:italic>in vivo</jats:italic>\n                    is assisted by molecular chaperones.\n                  </jats:p>\n                </jats:list-item>\n                <jats:list-item>\n                  <jats:p>Assisted protein folding requires ATP energy.</jats:p>\n                </jats:list-item>\n                <jats:list-item>\n                  <jats:p>Molecular chaperones are evolutionarily conserved.</jats:p>\n                </jats:list-item>\n                <jats:list-item>\n                  <jats:p>Chaperone activity is controlled by co‐chaperones and cofactors.</jats:p>\n                </jats:list-item>\n                <jats:list-item>\n                  <jats:p>Chaperone families differ in structure and function.</jats:p>\n                </jats:list-item>\n              </jats:list>\n            </jats:p>\n          </jats:sec>","journal":"Encyclopedia of Life Sciences","year":2010,"id":25004,"datarank":0.0,"base_score":0.0,"endowment":0.0,"self_citation_contribution":0.0,"citation_network_contribution":0.0,"self_endowment_contribution":0.0,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":0,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":141772,"name":"G Elif Karagöz","orcid":null,"position":1,"is_corresponding":false},{"id":141773,"name":"Stefan GD Rüdiger","orcid":null,"position":2,"is_corresponding":false},{"id":141771,"name":"Tessa Sinnige","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"24523987","pmcid":null,"openalex_id":"https://openalex.org/W2117300107","authors":[],"funders":[],"total_grants":0,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[],"oa_status":"closed","license":"http://doi.wiley.com/10.1002/tdm_license_1.1","oa_locations":[{"url":"https://onlinelibrary.wiley.com/doi/pdf/10.1002/9780470015902.a0005721.pub2","host_type":"publisher"},{"url":"https://onlinelibrary.wiley.com/doi/full-xml/10.1002/9780470015902.a0005721.pub2","host_type":"publisher"},{"url":"https://doi.org/10.1002/9780470015902.a0005721.pub2","host_type":"journal"}],"fields_of_study":["Heat shock proteins research","Endoplasmic Reticulum Stress and Disease","Protein Structure and Dynamics","Biology","Chemistry"],"mesh_terms":[],"keywords":["Co-chaperone","Chaperone (clinical)","Chaperonin","Protein folding","Chemical chaperone","Heat shock protein","Hsp90","Protein structure","Biology","Foldase","Hsp70","Biochemistry","Cell biology","Chemistry","GroEL","Unfolded protein response","Endoplasmic reticulum"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Responsible consumption and production"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-07T23:43:30.194858Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}