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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 PDFUnderstanding the Curvature Effect on the Structure and Bonding of MoC Nanoparticles on Carbon Supports.
ACS Appl Mater Interfaces
January 2025
Departament de Ciència de Materials i Química Física & Institut de Química Teòrica i Computacional (IQTCUB), Universitat de Barcelona, c/Martí i Franquès 1-11, Barcelona 08028, Spain.
The interaction between molybdenum carbide (MoC) nanoparticles and both flat and curved graphene surfaces, serving as models for carbon nanotubes, was investigated by means of density functional theory. A variety of MoC nanoparticles with different sizes and stoichiometries have been used to explore different adsorption sites and modes across models with different curvature degrees. On flat graphene, off-stoichiometric MoC featuring more low-coordinated Mo atoms exhibits stronger interaction and increased electron transfers from the carbide to the carbon substrate.
View Article and Find Full Text PDFThermal aggregation of immunoglobulin G depending on the charge state of protein-polyelectrolyte complexes.
Int J Biol Macromol
January 2025
Institute of Pure and Applied Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8573, Japan. Electronic address:
Protein-polyelectrolyte complexes (PPCs) exhibit opposite effects, both suppressing and promoting protein aggregation, depending on the type of components. For the application of PPCs as protein stabilization technology, these opposite effects must be controlled. In this study, we investigated the thermal aggregation of immunoglobulin G (IgG)-polyamino acid complexes to elucidate the relationship between the charge state of PPCs, evaluated by the zeta potential, and their opposite effects on the aggregation process, which were measured using a spectrophotometer.
View Article and Find Full Text PDFCharge Manipulation of Porous Coordination Cages Tunes the Efficiency and Selectivity in Electrochemical Synthesis.
Angew Chem Int Ed Engl
December 2024
State Key Laboratory of Chemo/Bio-Sensing and Chemometrics, College of Chemistry and Chemical Engineering, Hunan University, 410082, Changsha, Hunan, China.
Electrocatalytic synthesis of high-value chemicals has been attracting growing interest owing to its environmentally benign reaction pathways. Among these processes, the electrocatalytic reduction of nitrate (NO ) to ammonia (NH), known as NORR, and the oxidation of 5-hydroxymethylfurfural (HMFOR) stand out as two cornerstone reactions; yet, their efficiency and selectivity pose ongoing challenges. In this study, we introduce a charge manipulation approach for the design of highly efficient electrocatalysts tailored for the simultaneous coupling of NORR and HMFOR.
View Article and Find Full Text PDFThe impact of charge regulation and ionic intranuclear environment on the nucleosome core particle.
J Chem Phys
December 2024
Department of Biomedical Engineering, Northwestern University, Evanston, Illinois 60208, USA.
We theoretically investigate how the intranuclear environment influences the charge of a nucleosome core particle (NCP)-the fundamental unit of chromatin consisting of DNA wrapped around a core of histone proteins. The molecular-based theory explicitly considers the size, shape, conformation, charge, and chemical state of all molecular species-thereby linking the structural state with the chemical/charged state of the system. We investigate how variations in monovalent and divalent salt concentrations, as well as pH, affect the charge distribution across different regions of an NCP and quantify the impact of charge regulation.
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