{"doi":"10.1073/pnas.2114690119","title":"Atomic-resolution chemical characterization of (2x)72-kDa tryptophan synthase via four- and five-dimensional <sup>1</sup> H-detected solid-state NMR","abstract":"NMR chemical shifts provide detailed information on the chemical properties of molecules, thereby complementing structural data from techniques like X-ray crystallography and electron microscopy. Detailed analysis of protein NMR data, however, often hinges on comprehensive, site-specific assignment of backbone resonances, which becomes a bottleneck for molecular weights beyond 40 to 45 kDa. Here, we show that assignments for the (2x)72-kDa protein tryptophan synthase (665 amino acids per asymmetric unit) can be achieved via higher-dimensional, proton-detected, solid-state NMR using a single, 1-mg, uniformly labeled, microcrystalline sample. This framework grants access to atom-specific characterization of chemical properties and relaxation for the backbone and side chains, including those residues important for the catalytic turnover. Combined with first-principles calculations, the chemical shifts in the β-subunit active site suggest a connection between active-site chemistry, the electrostatic environment, and catalytically important dynamics of the portal to the β-subunit from solution.","journal":"Proceedings of the National Academy of Sciences","year":2022,"id":238435,"datarank":0.0,"base_score":0.0,"endowment":0.0,"self_citation_contribution":0.0,"citation_network_contribution":0.0,"self_endowment_contribution":0.0,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":54,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":0.8591,"is_data_producer":false,"deposit_databanks":null,"is_oa":true,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":"2022-01-01","fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":826238,"name":"Petra Rovó","orcid":"0000-0001-8729-7326","position":1,"is_corresponding":false},{"id":455591,"name":"Varun V. Sakhrani","orcid":null,"position":2,"is_corresponding":false},{"id":759372,"name":"Yangyang Wang","orcid":"0000-0001-7042-9804","position":3,"is_corresponding":false},{"id":759373,"name":"Jacob B. Holmes","orcid":"0000-0003-0137-8382","position":4,"is_corresponding":false},{"id":759371,"name":"Viktoriia Liu","orcid":"0000-0001-9803-5188","position":5,"is_corresponding":false},{"id":20982,"name":"Patricia Skowronek","orcid":"0000-0002-8441-6067","position":6,"is_corresponding":false},{"id":826239,"name":"Laura Kukuk","orcid":"0000-0002-4929-4156","position":7,"is_corresponding":false},{"id":826240,"name":"Suresh K. Vasa","orcid":"0000-0002-8137-9344","position":8,"is_corresponding":false},{"id":813436,"name":"Peter Güntert","orcid":"0000-0002-2911-7574","position":9,"is_corresponding":false},{"id":454378,"name":"Leonard J. Mueller","orcid":"0000-0002-2607-9875","position":10,"is_corresponding":false},{"id":826241,"name":"Rasmus Linser","orcid":"0000-0001-8983-2935","position":11,"is_corresponding":false},{"id":826237,"name":"Alexander Klein","orcid":"0000-0002-4963-1626","position":0,"is_corresponding":true}],"reference_count":91,"raw_metadata":null,"created_at":"2026-07-19T00:22:26.932537Z","pmid":"35058365","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":[]}