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Title: Characterization of Native Protein Complexes Using Ultraviolet Photodissociation Mass Spectrometry Open Access Deposited

https://creativecommons.org/licenses/by/3.0/us/
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Abstract
  • Ultraviolet photodissociation (UVPD) mass spectrometry (MS) was used to characterize the sequences of proteins in native protein-ligand and protein-protein complexes and to provide auxiliary information about the binding sites of the ligands and protein-protein interfaces. UVPD outperformed collisional induced dissociation (CID) and higher-energy collisional dissociation (HCD) in terms of yielding the most comprehensive diagnostic primary sequence information of the proteins in the complexes. UVPD also generated non-covalent fragment ions containing a portion of the protein still bound to the ligand which revealed some insight into the nature of the binding sites of myoglobin/heme, eIF4E/m7GTP, and as well as human peptidyl-prolyl cis-trans isomerase Pin1 in complex with the peptide derived from the C-terminal domain of RNA polymerase II. Non-covalently bound protein-protein fragment ions from oligomeric beta-lactoglobulin dimers and hexameric insulin complexes were also produced upon UVPD, providing some illumination of tertiary and quaternary protein structural features.
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  • 06/20/2024
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To Cite this Work:
Characterization of Native Protein Complexes Using Ultraviolet Photodissociation Mass Spectrometry [Data set]. Indiana University - DataCORE.

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Files (Count: 3; Size: 2.52 KB)

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Characterization_of_Native_Prote...t.zip 2024-08-16 2024-08-16 Open Access
Characterization_of_Native_Prote...t.txt 2024-08-16 2024-08-16 293 Bytes Open Access
README.txt 2024-08-16 2024-08-16 2.24 KB Open Access

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