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Pijning"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"software":[""],"submitter_keywords":["Human","Disulfide bonds","Fibrinogen"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD076459"],"tissue":["Blood Plasma"],"sample_protocol":["For some samples, dynabeads were coated with 16 μg of polyclonal anti-fibrinogen antibody in 1 mL of phosphate-buffered saline (PBS) on a rotating wheel for 1 h at 22°C and the excess antibody removed by washing three times with 1 mL of PBS. Plasma samples were incubated with 2 mg of coated beads on a rotating wheel for 1 h at 22°C. The beads were collected using a magnet and incubated in 0.3 mL of 4 mM 2-Iodo-N-phenylacetamide (12C-IPA) in PBS for 1 h at room temperature with gentle rotation, while kept away from light. Control samples of 5 μL plasma were also incubated with 4 mM 12C-IPA in the dark.  For some samples, thirty μM of GHRPLC or GPRPLC peptides was incubated with 20 μL of maleimide agarose in 0.5 mL of PBS with 1 mM ethylenediaminetetraacetic acid (EDTA) for 1 h with rotation on a wheel. Agarose was pelleted by centrifugation at 500g and washed with 0.5 mL of PBS three times prior to blocking for 1 h with 50 mM glutathione in PBS with 1 mM EDTA and three more washes with 0.5 mL of PBS. Control (no peptide) or peptide-labelled agarose was centrifuged, resuspended in 500 μL of plasma and incubated for 1 h with rotation at room temperature. The agarose was centrifuged, the beads washed three times in 0.5 mL of PBS and resuspended in 0.5 mL of 4 mM 2-Iodo-N-phenylacetamide (12C-IPA) in PBS for 1 h at room temperature with gentle rotation in the dark. Control samples of 5 μL plasma were also incubated with 4 mM 12C-IPA in the dark. In some cases, 10 μL of plasma was incubated with 280 μM, 560 μM, or 1.12 mM GHRP peptide in a total of 25 μL for 30 min.  The bead supernatants were aspirated, and all samples were incubated with NuPAGE LDS sample buffer (Life Technologies) containing a further 4 mM 12C-IPA for 30 min at 60°C. Samples were resolved on SDS-PAGE at 150 V for 65 min before gels were stained with colloidal Coomassie (Sigma) and destained in 7% acetic acid and 10% methanol. An example Coomassie gel is shown in Figure S1. Fibrinogen bands were excised, diced into 1 mm3 slices, destained in 25 mM NH4HCO3 with 50% acetonitrile, dried in 100% acetonitrile, incubated with 40 mM dithiothreitol and washed. The gel slices were incubated with 5 mM 13C-IPA (Cambridge Isotopes) in 25 mM NH4HCO3, with 10% DMSO for 1 h at room temperature in the dark to alkylate the disulfide bond cysteines. Gel slices were washed and dried as above before digestion of proteins with 35 μL of 12.5 ng/μL trypsin (Promega, V5280, Trypsin Gold, Mass spectrometry Grade) in 25 mM NH4HCO3 overnight at 30°C. Peptides were eluted from the slices with 5% formic acid and 50% acetonitrile.  Liquid chromatography, mass spectrometry and data analysis were performed as previously described (Al-Masri et al., 2023). Briefly, peptides were analyzed on a Thermo Fisher Scientific Ultimate 3000. Two hundred ng of peptide was injected and resolved on a 35 cm × 75 μm C18 reverse phase analytical column with integrated emitter using a 2 y-35% acetonitrile over 20 min with a flow rate of 250 nL/min. The peptides were ionized by electrospray ionization at +2.0 kV. Tandem mass spectrometry analysis was carried out on a Q-Exactive Plus mass spectrometer using HCD fragmentation. The data-dependent acquisition method acquired MS/MS spectra of the top 10 most abundant ions with charged states ≥2 at any one point during the gradient."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["MS/MS spectra were searched against the Swissprot reference proteome using Mascot search engine (Version 3.1, Matrix Science). Precursor mass tolerance and fragment tolerance were set at 10 ppm and the precursor ion charge state to 2+ and 3+. Variable modifications were defined as oxidized Met, deamidated Asn/Gln, N-terminal pyro Glu/Gln, Iodoacetanilide derivative cysteine and Iodoacetanilide-13C derivative cysteine with full trypsin cleavage and up to one missed cleavage. Only peptides with a peptide score ≥ 30 (p < 0.05) and error ≤6 ppm were selected for quantification of relative abundance. Ion chromatograms of peptides labeled with 12C-IPA and/or 13C-IPA were generated using FreeStyle software (Thermo Fisher). The area under the curve (AUC) of each peptide was calculated using the automated peak detection function built into Freestyle. The fraction of unformed disulfide bond was calculated as the AUC of 12C-IPA labeled peptide divided by the AUC of 12C-IPA plus 13C-IPA labeled peptides. The data was routinely searched for peptides containing unlabeled cysteine thiols and these were not detected, which indicates that alkylation of unpaired cysteine residues by 12C-IPA or 13C-IPA was complete in the protein."],"omics_type":["Proteomics"],"labhead":["Philip J. Hogg"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["School of Life Sciences, University of Technology Sydney, Faculty of Science, Sydney, New South Wales, Australia Centenary Institute, University of Sydney, Sydney, New South Wales, Australia"],"species":["Homo Sapiens (human)"],"publication":["41940651 Pijning AE, Butera D, Hogg PJ. Multiple disulfide-bonded states confer extensive conformational diversity in fibrinogen. Protein Sci. 2026 35(5):e70558 10.1002/pro.70558"],"submitter_mail":["a.pijning@centenary.org.au"],"submitter_affiliation":["Centenary Insitute, The University of Sydney"],"submitter_country":["Australia"],"doi":["10.6019/PXD076459"],"pubmed_abstract":["Disulfide bonds constrain the polypeptide backbone and reduce conformational variability in proteins. The blood clotting protein fibrinogen is constitutively produced as multiple partially disulfide-bonded states, suggesting that individual fibrinogen molecules have a variety of conformational forms. This hypothesis was tested by resolving fibrinogen molecules on beads coated with different fibrinogen ligands and measuring their disulfide states by differential cysteine alkylation and mass spectrometry. Polyclonal anti-fibrinogen antibodies resolved states where all 11 measured disulfides across the molecule were significantly less formed. In contrast, the GHRP peptide, which binds the fibrinogen β-nodule, resolved states in which seven β-nodule and central E region disulfides were significantly more formed, while the GPRP peptide, which binds the γ-nodule, resolved states in which only one disulfide was significantly more formed. To probe the link between disulfide state and conformation, in silico analysis of all 32 possible disulfide-bonded states of the β-nodule revealed that the conformational flexibility of this domain and predicted GHRP interactions in its binding pocket are predicated on the oxidation state of one of the five β-nodule disulfides, βC424-βC437. These findings indicate that the different disulfide-bonded states of fibrinogen adopt an extensive array of conformations that are selectively recognized by different fibrinogen ligands."],"pubmed_title":["Multiple disulfide-bonded states confer extensive conformational diversity in fibrinogen."],"pubmed_authors":["Pijning Aster E AE, Butera Diego D, Hogg Philip J PJ"],"additional_accession":[]},"is_claimable":false,"name":"Multiple disulfide-bonded states confer conformational diversity in fibrinogen","description":"Disulfide bonds constrain the polypeptide backbone and reduce conformational variability in proteins. The blood clotting protein fibrinogen is constitutively produced as multiple partially disulfide-bonded states, suggesting that individual fibrinogen molecules have a variety of conformational forms. This hypothesis was tested by resolving fibrinogen molecules on beads coated with different fibrinogen ligands and measuring their disulfide states by differential cysteine alkylation and mass spectrometry. Polyclonal anti-fibrinogen antibodies resolved states where all 11 measured disulfides across the molecule were significantly less formed. In contrast, the GHRP peptide, which binds the fibrinogen β-nodule, resolved states in which seven β-nodule and central E region disulfides were significantly more formed, while the GPRP peptide, which binds the γ-nodule, resolved states in which only one disulfide was significantly more formed. To probe the link between disulfide state and conformation, in silico analysis of all 32 possible disulfide-bonded states of the β-nodule revealed that the conformational flexibility of this domain and predicted GHRP interactions in its binding pocket are predicated on the oxidation state of one of the five β-nodule disulfides, βC424-βC437. These findings indicate that the different disulfide-bonded states of fibrinogen adopt an extensive array of conformations that are selectively recognized by different fibrinogen ligands.","dates":{"publication":"2026-04-13","submission":"2026-04-01"},"accession":"PXD076459","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2042546","NEWT:148942","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:44270","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:2433","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:11308","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1410384","NEWT:1310173","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:118221","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:1423687","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:1301262","NEWT:2305479","NEWT:215451","NEWT:460519","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2499525","NEWT:467144","NEWT:142786","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:272831","NEWT:987059","NEWT:491","NEWT:460523","NEWT:2423","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:291146","NEWT:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:2003758","NEWT:29486","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:1325292","NEWT:219798","NEWT:548","NEWT:150475","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:1225786","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:311339","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:536","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:116597","NEWT:353153","NEWT:116598","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:941638","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:6039","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:280406","NEWT:83906","NEWT:99488","NEWT:99487","NEWT:1134506","NEWT:255470","NEWT:762903","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:266940","NEWT:287889","NEWT:9938","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:483179","NEWT:315750","NEWT:99490","NEWT:632957","NEWT:11294","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:1479235","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:105812","NEWT:11298","NEWT:4233","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:487521","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:1170227","NEWT:2666255","NEWT:999810","NEWT:28995","NEWT:1392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