{"doi":"10.1016/j.abb.2014.07.017","title":"Folding energetics and oligomerization of polytopic α-helical transmembrane proteins","abstract":null,"journal":"Archives of Biochemistry and Biophysics","year":2014,"id":688551,"datarank":0.5289540786924243,"base_score":3.5263605246161616,"endowment":3.5263605246161616,"self_citation_contribution":0.5289540786924243,"citation_network_contribution":0.0,"self_endowment_contribution":0.5289540786924243,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":33,"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":1798842,"name":"Noreen Klein","orcid":null,"position":1,"is_corresponding":false},{"id":225461,"name":"Daniel E. Otzen","orcid":"0000-0002-2918-8989","position":2,"is_corresponding":false},{"id":472786,"name":"Dirk Schneider","orcid":"0000-0003-4517-6387","position":3,"is_corresponding":false},{"id":1798841,"name":"Jennifer Neumann","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Folding energetics and oligomerization of polytopic α-helical transmembrane proteins","abstract":"While interactions of single-span transmembrane helices have been studied to a significant extent in the past years, the folding of polytopic α-helical transmembrane proteins, as well as their oligomerization, are far less analyzed and understood. The goal of the few thus far performed thermodynamic studies, in which unfolding of polytopic TM proteins was described, was to achieve a mild, potentially reversible unfolding process, to finally derive thermodynamic parameters for the reverse folding pathway. In the first part of this review, we summarize the studies analyzing the thermodynamic stability and folding pathways of polytopic transmembrane proteins. Based on these studies, we deduce some common principles, guiding transmembrane protein unfolding and folding, important for the design of future folding/unfolding studies. Furthermore, the discussed observations can conceptually guide an experimental search for proper in vitro transmembrane protein refolding conditions. In many of the resolved membrane protein structures, individual monomers interact to form higher ordered oligomers. In most cases, oligomerization of those monomeric units appears to be intimately linked to the protein function, and folding of the individual protomers might even occur only after interaction. In the second part of this review, we discuss folding pathways of oligomeric α-helical transmembrane proteins as well as causes and consequences of α-helical transmembrane protein oligomerization.","is_dataset_classified":null,"base_score":3.5263605246161616,"endowment":3.5263605246161616,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"25057769","pmcid":null,"openalex_id":"https://openalex.org/W2093538782","authors":[],"funders":[{"funder_name":"Deutsche Forschungsgemeinschaft","grant_id":"unidentified","title":"unidentified"},{"funder_name":"German Chemical Industry Fund","grant_id":"","title":null},{"funder_name":"Stiftung Rheinland-Pfalz für Innovation","grant_id":"","title":null},{"funder_name":"Danish Research Foundation","grant_id":"","title":null},{"funder_name":"Danish Research Council|Natural Sciences","grant_id":"","title":null},{"funder_name":"Deutsche Forschungsgemeinschaft","grant_id":"","title":null}],"total_grants":6,"fwci":1.1369,"citation_percentile":0.73209412,"influential_citations":0,"citation_trend":[{"year":2014,"count":2},{"year":2015,"count":2},{"year":2016,"count":1},{"year":2017,"count":4},{"year":2018,"count":2},{"year":2019,"count":5},{"year":2020,"count":2},{"year":2021,"count":2},{"year":2022,"count":4},{"year":2023,"count":4},{"year":2024,"count":3},{"year":2025,"count":2}],"oa_status":"closed","license":"Elsevier TDM","oa_locations":[{"url":"https://api.elsevier.com/content/article/PII:S0003986114002689?httpAccept=text/plain","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0003986114002689?httpAccept=text/xml","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.abb.2014.07.017","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/25057769","host_type":"repository"},{"url":"https://pure.au.dk/portal/en/publications/7a269309-fe9f-4753-805c-547e171d557b","host_type":""},{"url":"https://dx.doi.org/10.1016/j.abb.2014.07.017","host_type":""}],"fields_of_study":["Photoreceptor and optogenetics research","Lipid Membrane Structure and Behavior","Photosynthetic Processes and Mechanisms","0301 basic medicine","0303 health sciences","03 medical and health sciences","Animals","Cell Membrane","Humans","Membrane Proteins","Protein Folding","Protein Multimerization","Protein Structure, Secondary"],"mesh_terms":["Animals","Cell Membrane","Humans","Membrane Proteins","Protein Structure, Secondary","Protein Folding","Protein Multimerization"],"keywords":["Energetics","Folding (DSP implementation)","Transmembrane protein","Protein folding","Chemistry","Biophysics","Transmembrane domain","Crystallography","Biology","Biochemistry","Membrane","Ecology","Membrane protein","Oligomerization","Folding Energetics","Cell Membrane","Animals","Humans","Membrane Proteins","Protein Multimerization","Protein Structure, Secondary"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-19T17:23:16.424876Z","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":[]}