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Characterization of native protein complexes using ultraviolet photodissociation mass spectrometry
- Source :
- Journal of the American Chemical Society. 136(37)
- Publication Year :
- 2014
-
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), higher-energy collisional dissociation (HCD), and electron transfer dissociation (ETD) in terms of yielding the most comprehensive diagnostic primary sequence information about the proteins in the complexes. UVPD also generated noncovalent 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/m(7)GTP, and human peptidyl-prolyl cis-trans isomerase 1 (Pin1) in complex with the peptide derived from the C-terminal domain of RNA polymerase II (CTD). Noncovalently bound protein-protein fragment ions from oligomeric β-lactoglobulin dimers and hexameric insulin complexes were also produced upon UVPD, providing some illumination of tertiary and quaternary protein structural features.
- Subjects :
- Models, Molecular
Stereochemistry
Ultraviolet Rays
Molecular Sequence Data
Analytical chemistry
Peptide
Heme
Lactoglobulins
Mass spectrometry
Crystallography, X-Ray
Ligands
Biochemistry
Catalysis
Dissociation (chemistry)
Mass Spectrometry
Article
chemistry.chemical_compound
Colloid and Surface Chemistry
Animals
Humans
Amino Acid Sequence
Horses
Binding site
Peptide sequence
chemistry.chemical_classification
Binding Sites
Myoglobin
Photodissociation
Proteins
General Chemistry
Peptidylprolyl Isomerase
Photochemical Processes
Electron-transfer dissociation
Eukaryotic Initiation Factor-4E
chemistry
Cattle
Protein Multimerization
Protein Binding
Subjects
Details
- ISSN :
- 15205126
- Volume :
- 136
- Issue :
- 37
- Database :
- OpenAIRE
- Journal :
- Journal of the American Chemical Society
- Accession number :
- edsair.doi.dedup.....586612bdf3330c4baaa2e023ac1c4ba7