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The kinetic methods generally employed for studying folding are typically limited to the time range of &gt; or = 1 ms because the folding of denatured proteins is usually initiated by mixing them with buffers that favor folding, and the dead time of rapid mixing experiments is about a millisecond. We now show that the study of protein folding may be extended to the microsecond time region by using temperature-jump measurements on the cold-unfolded state of a suitable protein. We are able to detect early events in the folding of mutants of barstar, the polypeptide inhibitor of barnase. A preliminary characterization of the fast phase from spectroscopic and phi-value analysis indicates that it is a transition between two relatively solvent-exposed states with little consolidation of structure.</jats:p>","is_dataset_classified":null,"base_score":4.927253685157205,"endowment":4.927253685157205,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"7479862","pmcid":"PMC40673","openalex_id":"https://openalex.org/W1977237286","authors":[],"funders":[],"total_grants":0,"fwci":5.6059,"citation_percentile":0.96848251,"influential_citations":0,"citation_trend":[{"year":2012,"count":2},{"year":2013,"count":5},{"year":2014,"count":2},{"year":2015,"count":4},{"year":2016,"count":1},{"year":2017,"count":1},{"year":2018,"count":2},{"year":2019,"count":2},{"year":2020,"count":5},{"year":2022,"count":1},{"year":2025,"count":1},{"year":2026,"count":1}],"oa_status":"green","license":null,"oa_locations":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/40673","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/40673","host_type":"repository"},{"url":"https://pnas.org/doi/pdf/10.1073/pnas.92.23.10668","host_type":"publisher"},{"url":"https://doi.org/10.1073/pnas.92.23.10668","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/7479862","host_type":"repository"},{"url":"http://europepmc.org/pmc/articles/PMC40673","host_type":"repository"}],"fields_of_study":["Protein Structure and Dynamics","Enzyme Structure and Function","Mass Spectrometry Techniques and Applications","Bacterial Proteins","Circular Dichroism","Enzyme Inhibitors","Kinetics","Models, Chemical","Mutation","Protein Denaturation","Protein Folding","Recombinant Proteins","Spectrometry, Fluorescence","Spectrophotometry"],"mesh_terms":["Bacterial Proteins","Circular Dichroism","Enzyme Inhibitors","Kinetics","Models, Chemical","Mutation","Protein Denaturation","Recombinant Proteins","Spectrometry, Fluorescence","Spectrophotometry","Protein Folding"],"keywords":["Barnase","Phi value analysis","Downhill folding","Protein folding","Microsecond","Chemistry","Contact order","Folding (DSP implementation)","Crystallography","Biophysics","Chemical physics","Biology","Physics","Biochemistry"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-16T20:46:56.173106Z","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":[]}