{"doi":"10.1002/prot.26547","title":"Protein–protein association properties of human\n                    <scp>βB2</scp>\n                    ‐crystallins","abstract":"<jats:title>Abstract</jats:title>\n                  <jats:p>Protein–protein association events are involved in many physiological and pathological processes. Cataract disease is a pathology that manifests protein aggregation of crystallins. β‐Crystallins are present in a high proportion in the eye lens. Therefore, the structural study of the dimerization properties of crystallins can shed light on the first stages of protein aggregation. In the present work, we examine the protein–protein association profiles of the human βB2‐crystallin by employing extensive coarse‐grained molecular dynamics (CG‐MD) and the Markov state analysis. Interestingly, our results clearly show important changes in the protein dimerization kinetics between wt‐HβB2C and the deamidated systems. The two systems show dimeric conformations. However, the association and dissociation rates are very different. Our results show that the deamidated system can associate faster and dissociate slower than the wt‐ HβB2C. The deamidated system is in a slightly opened conformation with the Greek‐key motifs well folded, suggesting that a complete unfolding of the protein is not required for aggregation. Our results describe the first stages of crystallin aggregation due to post‐translational modifications.</jats:p>","journal":"Proteins: Structure, Function, and Bioinformatics","year":2025,"id":24990,"datarank":0.11928060897526875,"base_score":0.6931471805599453,"endowment":0.6931471805599453,"self_citation_contribution":0.10397207708399181,"citation_network_contribution":0.015308531891276936,"self_endowment_contribution":0.10397207708399181,"citer_contribution":0.015308531891276936,"corpus_percentile":null,"corpus_rank":null,"citation_count":1,"citer_count":1,"citers_with_citation_signal":1,"citers_with_endowment":1,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":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":148325,"name":"Laura Domínguez","orcid":"0000-0003-3666-2789","position":1,"is_corresponding":false},{"id":148324,"name":"José‐Luis Velasco‐Bolom","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":0.6931471805599453,"endowment":0.6931471805599453,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"37455623","pmcid":"PMC12260336","openalex_id":"https://openalex.org/W4384493370","authors":[],"funders":[{"funder_name":"Consejo Nacional de Ciencia y Tecnología, Paraguay","grant_id":"445924/29330","title":null},{"funder_name":"Dirección General de Cómputo y de Tecnologías de Información","grant_id":"LANCAD-UNAM-DGTIC-306","title":null},{"funder_name":"Programa de Apoyo a la Investigación y el Posgrado","grant_id":"PAIP 5000-9155","title":null},{"funder_name":"Programa de Apoyo a Proyectos de Investigación e Innovación Tecnológica","grant_id":"PAPIIT IN221620","title":null}],"total_grants":4,"fwci":0.1454,"citation_percentile":0.5809329,"influential_citations":0,"citation_trend":[{"year":2025,"count":1}],"oa_status":"hybrid","license":"cc-by","oa_locations":[{"url":"https://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/prot.26547","host_type":"journal"},{"url":"https://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/prot.26547","host_type":"HYBRID"},{"url":"https://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/prot.26547","host_type":"publisher"},{"url":"https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.26547","host_type":"publisher"},{"url":"https://doi.org/10.1002/prot.26547","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/37455623","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/12260336","host_type":"repository"},{"url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC12260336/pdf/PROT-93-1361.pdf","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC12260336","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC12260336?pdf=render","host_type":"Europe_PMC"}],"fields_of_study":["Connexins and lens biology","Protein Structure and Dynamics","Heat shock proteins research","Medicine","Biology","Materials Science","Chemistry","Humans","Molecular Dynamics Simulation","Protein Multimerization","beta-Crystallin B Chain","Kinetics","Protein Binding","Markov Chains","Protein Processing, Post-Translational","Protein Conformation","Protein Aggregates"],"mesh_terms":["Humans","Kinetics","Markov Chains","Protein Binding","Protein Conformation","Protein Processing, Post-Translational","beta-Crystallin B Chain","Protein Multimerization","Molecular Dynamics Simulation","Protein Aggregates"],"keywords":["Crystallin","Protein aggregation","Chemistry","Dissociation (chemistry)","Kinetics","Biophysics","Biochemistry","Biology","Cataract","Molecular dynamics","Deamidation","Markov State Model","Coarse‐grained","Βb2‐crystallins"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-07T23:41:51.360157Z","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":[]}