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[Vacuum ultraviolet laser dissociation and proteomic analysis of halogenated peptides].
Se Pu
February 2025
CAS Key Laboratory of Separation Sciences for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China.
Chemical modifications are widely used in research fields such as quantitative proteomics and interaction analyses. Chemical-modification targets can be roughly divided into four categories, including those that integrate isotope labels for quantification purposes, probe the structures of proteins through covalent labeling or cross-linking, incorporate labels to improve the ionization or dissociation of characteristic peptides in complex mixtures, and affinity-enrich various poorly abundant protein translational modifications (PTMs). A chemical modification reaction needs to be simple and efficient for use in proteomics analysis, and should be performed without any complicated process for preparing the labeling reagent.
View Article and Find Full Text PDFStructural Analysis of the 20S Proteasome Using Native Mass Spectrometry and Ultraviolet Photodissociation.
J Proteome Res
December 2024
Department of Chemistry, The University of Texas at Austin, Austin, Texas 78712, United States.
Owing to the role of the 20S proteasome in a wide spectrum of pathologies, including neurodegenerative disorders, proteasome-associated autoinflammatory syndromes (PRAAS), and cardiovascular diseases, understanding how its structure and composition contribute to dysfunction is crucial. As a 735 kDa protein assembly, the 20S proteasome facilitates normal cellular proteostasis by degrading oxidized and misfolded proteins. Declined proteasomal activity, which can be attributed to perturbations in the structural integrity of the 20S proteasome, is considered one of the main contributors to multiple proteasome-related diseases.
View Article and Find Full Text PDFCharacterization of a Monoclonal Antibody by Native and Denaturing Top-Down Mass Spectrometry.
J Am Soc Mass Spectrom
September 2024
Department of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.
Established in recent years as an important approach to unraveling the heterogeneity of intact monoclonal antibodies, native mass spectrometry has been rarely utilized for sequencing these complex biomolecules via tandem mass spectrometry. Typically, top-down mass spectrometry has been performed starting from highly charged precursor ions obtained via electrospray ionization under denaturing conditions (i.e.
View Article and Find Full Text PDFGlycoproteomics: Charting new territory in mass spectrometry and glycobiology.
J Mass Spectrom
June 2024
Department of Chemistry, Yale University, New Haven, Connecticut, USA.
Glycosylation is an incredibly common and diverse post-translational modification that contributes widely to cellular health and disease. Mass spectrometry is the premier technique to study glycoproteins; however, glycoproteomics has lagged behind traditional proteomics due to the challenges associated with studying glycosylation. For instance, glycans dissociate by collision-based fragmentation, thus necessitating electron-based fragmentation for site-localization.
View Article and Find Full Text PDFToward Better Pedestrian Trajectory Predictions: The Role of Density and Time-to-Collision in Hybrid Deep-Learning Algorithms.
Sensors (Basel)
April 2024
Department for Traffic Safety and Reliability, University of Wuppertal, 42119 Wuppertal, Germany.
Predicting human trajectories poses a significant challenge due to the complex interplay of pedestrian behavior, which is influenced by environmental layout and interpersonal dynamics. This complexity is further compounded by variations in scene density. To address this, we introduce a novel dataset from the Festival of Lights in Lyon 2022, characterized by a wide range of densities (0.
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