{"doi":"10.47583/ijpsrr.2021.v69i02.002","title":"Modalities of Protein Denaturation and Nature of Denaturants","abstract":"<jats:p>Denaturation of protein is a biological phenomenon in which a protein loses its native shape due to the breaking or disruption of\nweak chemical bonds and interactions which makes the protein biologically inactive. It is the process where properly folded proteins\nformed under physiological conditions is transformed to an unfolded protein under non-physiological conditions. The process of denaturation of proteins can occur under different physiological and chemical conditions. Denaturation can be reversible or\nirreversible. Denaturation mostly takes places when the protein is subjected under external elements like inorganic solutes, organic\nsolvents, acids or bases, and by heat or irradiations. The denaturing agents or denaturants widely used in protein folding or unfolding\nexperiments are urea and guanidinium chloride (GdmCl). In denaturation, the alpha-helix structure and beta sheets structure of the native protein are disrupted and unfolds it into any random shape. We can also say that denaturation occurs due to the disruption of bonding interactions which are responsible for secondary structure and the tertiary structure of the proteins.</jats:p>","journal":"International Journal of Pharmaceutical Sciences Review and Research","year":2021,"id":666144,"datarank":0.611630616585858,"base_score":4.07753744390572,"endowment":4.07753744390572,"self_citation_contribution":0.611630616585858,"citation_network_contribution":0.0,"self_endowment_contribution":0.611630616585858,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":58,"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":1739600,"name":"Pratima Chaudhuri","orcid":null,"position":1,"is_corresponding":false},{"id":1739598,"name":"Vaishali V. Acharya","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Modalities of Protein Denaturation and Nature of Denaturants","abstract":"<jats:p>Denaturation of protein is a biological phenomenon in which a protein loses its native shape due to the breaking or disruption of\nweak chemical bonds and interactions which makes the protein biologically inactive. It is the process where properly folded proteins\nformed under physiological conditions is transformed to an unfolded protein under non-physiological conditions. The process of denaturation of proteins can occur under different physiological and chemical conditions. Denaturation can be reversible or\nirreversible. Denaturation mostly takes places when the protein is subjected under external elements like inorganic solutes, organic\nsolvents, acids or bases, and by heat or irradiations. The denaturing agents or denaturants widely used in protein folding or unfolding\nexperiments are urea and guanidinium chloride (GdmCl). In denaturation, the alpha-helix structure and beta sheets structure of the native protein are disrupted and unfolds it into any random shape. We can also say that denaturation occurs due to the disruption of bonding interactions which are responsible for secondary structure and the tertiary structure of the proteins.</jats:p>","is_dataset_classified":null,"base_score":4.07753744390572,"endowment":4.07753744390572,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"19162232","pmcid":null,"openalex_id":"https://openalex.org/W3197201247","authors":[],"funders":[],"total_grants":0,"fwci":2.9153,"citation_percentile":0.92828595,"influential_citations":0,"citation_trend":[{"year":2022,"count":4},{"year":2023,"count":8},{"year":2024,"count":18},{"year":2025,"count":18},{"year":2026,"count":10}],"oa_status":"gold","license":"http://creativecommons.org/licenses/by-nc-nd/4.0","oa_locations":[{"url":"https://doi.org/10.47583/ijpsrr.2021.v69i02.002","host_type":"journal"},{"url":"https://doi.org/10.47583/ijpsrr.2021.v69i02.002","host_type":"publisher"},{"url":"https://globalresearchonline.net/journalcontents/v69-2/02.pdf","host_type":"publisher"}],"fields_of_study":["Mass Spectrometry Techniques and Applications","Protein Structure and Dynamics","Enzyme Structure and Function"],"mesh_terms":[],"keywords":["Denaturation (fissile materials)","Guanidinium chloride","Chemistry","Protein folding","Biophysics","Protein secondary structure","Protein structure","Urea","Crystallography","Folding (DSP implementation)","Protein tertiary structure","Helix (gastropod)","Biochemistry","Biology","Enzyme"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-13T13:28:08.353109Z","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":[]}