{"doi":"10.1021/ja301681v","title":"Using Thioamides To Site-Specifically Interrogate the Dynamics of Hydrogen Bond Formation in β-Sheet Folding","abstract":null,"journal":"Journal of the American Chemical Society","year":2012,"id":670994,"datarank":3.5897902384877796,"base_score":4.290459441148391,"endowment":4.290459441148391,"self_citation_contribution":0.6435689161722588,"citation_network_contribution":2.946221322315521,"self_endowment_contribution":0.6435689161722588,"citer_contribution":2.946221322315521,"corpus_percentile":null,"corpus_rank":null,"citation_count":72,"citer_count":67,"citers_with_citation_signal":66,"citers_with_endowment":66,"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":733706,"name":"Hyunil Jo","orcid":"0000-0002-4863-0779","position":1,"is_corresponding":false},{"id":239680,"name":"William F. DeGrado","orcid":"0000-0003-4745-263X","position":2,"is_corresponding":false},{"id":180495,"name":"Feng Gai","orcid":"0000-0003-1621-7119","position":3,"is_corresponding":false},{"id":1752858,"name":"Robert M. Culik","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Using Thioamides To Site-Specifically Interrogate the Dynamics of Hydrogen Bond Formation in β-Sheet Folding","abstract":"Thioamides are sterically almost identical to their oxoamide counterparts, but they are weaker hydrogen bond acceptors. Therefore, thioamide amino acids are excellent candidates for perturbing the energetics of backbone-backbone H-bonds in proteins and hence should be useful in elucidating protein folding mechanisms in a site-specific manner. Herein, we validate this approach by applying it to probe the dynamic role of interstrand H-bond formation in the folding kinetics of a well-studied β-hairpin, tryptophan zipper. Our results show that reducing the strength of the peptide's backbone-backbone H-bonds, except the one directly next to the β-turn, does not change the folding rate, suggesting that most native interstrand H-bonds in β-hairpins are formed only after the folding transition state.","is_dataset_classified":null,"base_score":4.290459441148391,"endowment":4.290459441148391,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"22540162","pmcid":"PMC3354031","openalex_id":"https://openalex.org/W2072502724","authors":[],"funders":[{"funder_name":"NIGMS NIH HHS","grant_id":"GM-065978","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"T32 GM008275","title":null},{"funder_name":"NIA NIH HHS","grant_id":"F31 AG039253","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM065978","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"GM-008275","title":null}],"total_grants":5,"fwci":2.8241,"citation_percentile":0.91408322,"influential_citations":0,"citation_trend":[{"year":2012,"count":6},{"year":2013,"count":6},{"year":2014,"count":6},{"year":2015,"count":5},{"year":2016,"count":11},{"year":2017,"count":7},{"year":2018,"count":4},{"year":2019,"count":6},{"year":2020,"count":3},{"year":2021,"count":6},{"year":2022,"count":1},{"year":2023,"count":3},{"year":2024,"count":5},{"year":2025,"count":2},{"year":2026,"count":1}],"oa_status":"closed","license":null,"oa_locations":[{"url":"https://pubs.acs.org/doi/pdf/10.1021/ja301681v","host_type":"publisher"},{"url":"https://doi.org/10.1021/ja301681v","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/22540162","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/3354031","host_type":"repository"}],"fields_of_study":["Protein Structure and Dynamics","Chemical Synthesis and Analysis","Enzyme Structure and Function","Amino Acid Sequence","Hydrogen Bonding","Models, Molecular","Peptide Fragments","Protein Folding","Protein Structure, Secondary","Protein Unfolding","Thioamides","Time Factors"],"mesh_terms":["Amino Acid Sequence","Hydrogen Bonding","Models, Molecular","Peptide Fragments","Thioamides","Time Factors","Protein Structure, Secondary","Protein Folding","Protein Unfolding"],"keywords":["Chemistry","Thioamide","Folding (DSP implementation)","Hydrogen bond","Steric effects","Zipper","Peptide bond","Kinetics","Tryptophan","Phi value analysis","Protein folding","Crystallography","Turn (biochemistry)","Stereochemistry","Amino acid","Molecule","Organic chemistry","Biochemistry"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-16T00:54:11.901800Z","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":[]}