{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Feldman D"],"funding":["NIA NIH HHS","NIAID NIH HHS","NCI NIH HHS","NIGMS NIH HHS"],"pubmed_abstract":["Library screening and selection methods can determine the binding activities of individual members of large protein libraries given a physical link between protein and nucleotide sequence, which enables identification of functional molecules by DNA sequencing. However, the solution properties of individual protein molecules cannot be probed using such approaches because they are completely altered by DNA attachment. Mass spectrometry enables parallel evaluation of protein properties amenable to physical fractionation such as solubility and oligomeric state, but current approaches are limited to libraries of 1,000 or fewer proteins. Here, we improved mass spectrometry barcoding by co-synthesizing proteins with barcodes optimized to be highly multiplexable and minimally perturbative, scaling"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2025.02.24.639402"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11888366"],"repository":["biostudies-literature"],"pubmed_title":["Massively parallel assessment of designed protein solution properties using mass spectrometry and peptide barcoding."],"pmcid":["PMC11888366"],"funding_grant_id":["R01 AI160052","U19 AG065156","P30 GM133893","R01 CA240339","P30 GM124169","R01 AG063845"],"pubmed_authors":["Eisenach H","Feldman D","Johnson R","Baker D","MacCoss MJ","Sims JN","Wicky BIM","Goreshnik I","Milles LF","Richardson C","Brackenbrough E","Lubner JM","Kang A","Stewart L","Vafeados D","Koepnick B","Bera AK","Sankaran B","Kim DE","Allen A","Gerben S","Hicks DR","Li X","Yang EC","Joyce E"],"additional_accession":[]},"is_claimable":false,"name":"Massively parallel assessment of designed protein solution properties using mass spectrometry and peptide barcoding.","description":"Library screening and selection methods can determine the binding activities of individual members of large protein libraries given a physical link between protein and nucleotide sequence, which enables identification of functional molecules by DNA sequencing. However, the solution properties of individual protein molecules cannot be probed using such approaches because they are completely altered by DNA attachment. Mass spectrometry enables parallel evaluation of protein properties amenable to physical fractionation such as solubility and oligomeric state, but current approaches are limited to libraries of 1,000 or fewer proteins. Here, we improved mass spectrometry barcoding by co-synthesizing proteins with barcodes optimized to be highly multiplexable and minimally perturbative, scaling","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Feb","modification":"2026-05-22T03:12:36.359Z","creation":"2025-04-04T01:28:39.516Z"},"accession":"S-EPMC11888366","cross_references":{"pubmed":["40060547"],"doi":["10.1101/2025.02.24.639402"]}}