{"database":"panorama","file_versions":[],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Jeremiah Sims"],"species":["Escherichia Coli Bl21(de3)"],"full_dataset_link":["https://panoramaweb.org/zynVcE.url"],"submitter_email":["simsjn@uw.edu"],"submitter_affiliation":["University of Washington"],"sample_protocol":[""],"repository":["PanoramaPublic"],"data_protocol":[""],"name_synonyms":["Mass Spectrum Analysis, Mass Spectrum, peptides, Analyses, protein complex, Proteins, Spectrometry, Gene, protein, Spectrum Analyses, protein-containing complex, Spectrum Analysis, Solution, Protein Gene Products, Spectroscopy, Gene Proteins, polypeptide, peptide, Polypeptides, MS, native protein, peptido, Protein, Gene Products, Mass, Peptid, peptidos, Polypeptide, Analysis, protein aggregate, Peptide., Mass Spectrum Analyses, Mass Spectroscopy"],"description_synonyms":["Solubilities, Carrier Protein, DNS, Procedures, (Deoxyribonucleotide)n, determination, acetylglucosaminyltransferase-like protein, Processes, Transport Proteins., selection process, Sequence Determination, RNA Sequence, Mbp1, Gene, protein, neutral molecular compounds, Spectrum Analyses, protein-containing complex, LARGE1, froggy, Deoxyribonucleic acids, Gyltl1a, Techniques, Deoxyribonucleic Acid, utilization, Method, symptoms, Mass, Studies, Gene Products, Screening, Analysis, protein aggregate, myd, Technique, molecule, Mass Spectroscopy, molecula, Mass Spectrum Analysis, thymus nucleic acid, molecules, like-acetylglucosaminyltransferase, Analyses, Determination, MDDGB6, ligand, Mbp-1, Double Stranded, LARGE, Deoxyribonucleic acid, procedures, Molekuel, Base Sequences, Sequence Determinations, Sequencing, Solution, Study, BPFD#36, DNA Sequence Analysis, Methodological Studies, scientific observation, Double-Stranded DNA, (Deoxyribonucleotide)m, deoxyribonucleic acids, DNAn, Nucleotide, Behaviors, Sequence Analyses, single-organism behavior, screening, measuring, RNA, use, findings, Process, gyltl1b-b, protein complex, statistics and numerical data, Nucleotide Sequences, DNAn+1, Proteins, Double-Stranded, Procedure, Carrier, Spectrum Analysis, Acceptance Processes, Determinations, (Deoxyribonucleotide)n+m, Spectroscopy, Sequences, Acceptance Process, MS, Screenings, native protein, Mass Screenings, Sequence, MDDGA6, mKIAA0609, DNA Sequencing, Protein, chemical analysis, DNA Sequence Determinations, numerical data, techniques, DNA Sequence, ds-DNA, KIAA0609, desoxyribose nucleic acid, Binding Protein, Library, acetylglucosaminyltransferase-like 1A, Mass Spectrum Analyses, RNA Sequences, DNA sequencing, fg, Mass Spectrum, Acceptance, Transport Protein, gyltl1b, mdc1d, Spectrometry, signs, Methodological, Methodological Study, LARGE_HUMAN, DNA Sequence Determination, Protein Gene Products, Gene Proteins, MDC1D, DNA Sequence Analyses, like-glycosyltransferase, enr, Base, ds DNA, Desoxyribonukleinsaeure, assay, DNA, DNA Sequences, Binding Proteins, methodology, glycosyltransferase-like protein LARGE1, Nucleotide Sequence"],"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 to libraries of >5,000 proteins. We use these barcodes together with mass spectrometry to assay the solution behavior of libraries of de novo-designed monomeric scaffolds, oligomers, binding proteins and nanocages, rapidly identifying design failure modes and successes.","dates":{"publication":"Tue Dec 24 00:00:00 GMT 2024"},"accession":"PXD059224","cross_references":{"TAXONOMY":["469008"]}}