{"doi":"10.1016/j.ab.2015.07.013","title":"Denatured state aggregation parameters derived from concentration dependence of protein stability","abstract":null,"journal":"Analytical Biochemistry","year":2015,"id":628629,"datarank":0.5533319181170905,"base_score":3.6888794541139363,"endowment":3.6888794541139363,"self_citation_contribution":0.5533319181170905,"citation_network_contribution":0.0,"self_endowment_contribution":0.5533319181170905,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":39,"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":1627648,"name":"Benjamin R. Clarkson","orcid":null,"position":1,"is_corresponding":false},{"id":1627649,"name":"Rogelio Siles","orcid":null,"position":2,"is_corresponding":false},{"id":960385,"name":"Patrick Ross","orcid":"0000-0003-1264-2273","position":3,"is_corresponding":false},{"id":1098041,"name":"Richard K. Brown","orcid":null,"position":4,"is_corresponding":false},{"id":934878,"name":"Ernesto Freire","orcid":"0000-0002-2335-6419","position":5,"is_corresponding":false},{"id":229152,"name":"Arne Schön","orcid":"0000-0002-2015-2090","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Denatured state aggregation parameters derived from concentration dependence of protein stability","abstract":"Protein aggregation is a major issue affecting the long-term stability of protein preparations. Proteins exist in equilibrium between the native and denatured or partially denatured conformations. Often denatured or partially denatured conformations are prone to aggregate because they expose to solvent the hydrophobic core of the protein. The aggregation of denatured protein gradually shifts the protein equilibrium toward increasing amounts of denatured and ultimately aggregated protein. Recognizing and quantitating the presence of denatured protein and its aggregation at the earliest possible time will bring enormous benefits to the identification and selection of optimal solvent conditions or the engineering of proteins with the best stability/aggregation profile. In this article, a new approach that allows simultaneous determination of structural stability and the amount of denatured and aggregated protein is presented. This approach is based on the analysis of the concentration dependence of the Gibbs energy (ΔG) of protein stability. It is shown that three important quantities can be evaluated simultaneously: (i) the population of denatured protein, (ii) the population of aggregated protein, and (iii) the fraction of denatured protein that is aggregated.","is_dataset_classified":null,"base_score":3.6888794541139363,"endowment":3.6888794541139363,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"26239214","pmcid":null,"openalex_id":"https://openalex.org/W1042862341","authors":[],"funders":[{"funder_name":"National Science Foundation","grant_id":"MCB-1157506","title":null}],"total_grants":1,"fwci":1.654,"citation_percentile":0.82987538,"influential_citations":0,"citation_trend":[{"year":2015,"count":1},{"year":2016,"count":1},{"year":2017,"count":3},{"year":2018,"count":7},{"year":2019,"count":5},{"year":2020,"count":1},{"year":2021,"count":3},{"year":2022,"count":3},{"year":2024,"count":7},{"year":2025,"count":7},{"year":2026,"count":1}],"oa_status":"closed","license":"http://www.elsevier.com/open-access/userlicense/1.0/","oa_locations":[{"url":"https://api.elsevier.com/content/article/PII:S0003269715003632?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0003269715003632?httpAccept=text/plain","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.ab.2015.07.013","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/26239214","host_type":"repository"}],"fields_of_study":["Protein purification and stability","Protein Structure and Dynamics","Enzyme Structure and Function","Animals","Antineoplastic Agents","Arginine","Carbonic Anhydrase II","Cattle","Cetuximab","Drug Stability","Enzyme Stability","Hot Temperature","Indicators and Reagents","Models, Molecular","Osmolar Concentration","Platelet Aggregation","Protein Aggregates","Protein Conformation","Protein Denaturation","Protein Stability","Solubility","Thermodynamics","Trastuzumab","Urea"],"mesh_terms":["Cetuximab","Trastuzumab","Animals","Antineoplastic Agents","Arginine","Cattle","Drug Stability","Enzyme Stability","Hot Temperature","Indicators and Reagents","Models, Molecular","Osmolar Concentration","Platelet Aggregation","Protein Conformation","Protein Denaturation","Solubility","Thermodynamics","Urea","Carbonic Anhydrase II","Protein Stability","Protein Aggregates"],"keywords":["Protein aggregation","Chemistry","Protein stability","Population","Denaturation (fissile materials)","Protein folding","Native state","Protein structure","Chromatography","Crystallography","Biochemistry","Denatured State Aggregation","Isothermal Chemical Denaturation","Protein Conformational Equilibrium","Thermodynamic Linkage Equilibrium And Aggregation"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-05T14:22:23.293217Z","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":[]}