Charge site assignment in native proteins by ultraviolet photodissociation (UVPD) mass spectrometry - Wikidata - wikimedia - TriplyDB

Charge site assignment in native proteins by ultraviolet photodissociation (UVPD) mass spectrometry

Charge site assignment in native proteins by ultraviolet photodissociation (UVPD) mass spectrometry

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The Mechanism Behind Top-Down UVPD Experiments: Making Sense of Apparent Contradictions.High-Throughput Analysis of Intact Human Proteins Using UVPD and HCD on an Orbitrap Mass Spectrometer.193 nm Ultraviolet Photodissociation Mass Spectrometry of Tetrameric Protein Complexes Provides Insight into Quaternary and Secondary Protein Topology.Photoelectron Transfer Dissociation Reveals Surprising Favorability of Zwitterionic States in Large Gaseous Peptides and Proteins Activated Ion-Electron Transfer Dissociation Enables Comprehensive Top-Down Protein Fragmentation.A comparative VUV absorption mass-spectroscopy study on protonated peptides of different size.Radical solutions: Principles and application of electron-based dissociation in mass spectrometry-based analysis of protein structure.Characterization of hydrogen bonding motifs in proteins: hydrogen elimination monitoring by ultraviolet photodissociation mass spectrometry.UV-POSIT: Web-Based Tools for Rapid and Facile Structural Interpretation of Ultraviolet Photodissociation (UVPD) Mass Spectra.Characterization of trimethoprim resistant E. coli dihydrofolate reductase mutants by mass spectrometry and inhibition by propargyl-linked antifolates.

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Charge site assignment in native proteins by ultraviolet photodissociation (UVPD) mass spectrometry

http://www.wikidata.org/entity/Q41982077

description

2015 nî lūn-bûn

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2015年の論文

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2015年论文

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name

Charge site assignment in nati ...... ation (UVPD) mass spectrometry

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Charge site assignment in nati ...... ation (UVPD) mass spectrometry

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Charge site assignment in nati ...... ation (UVPD) mass spectrometry

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Charge site assignment in nati ...... ation (UVPD) mass spectrometry

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Jennifer S Brodbelt

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Lindsay J Morrison

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P2860

New reagents for increasing ESI multiple charging of proteins and protein complexes

Functional implications of structural differences between variants A and B of bovine beta-lactoglobulin.

Crystal structures of bovine beta-lactoglobulin in the orthorhombic space group C222(1). Structural differences between genetic variants A and B and features of the Tanford transition

Scalable molecular dynamics with NAMD

Electrospray ionization for mass spectrometry of large biomolecules

Collisional and Coulombic unfolding of gas-phase proteins: high correlation to their domain structures in solution.

A uniform field ion mobility study of melittin and implications of low-field mobility for resolving fine cross-sectional detail in peptide and protein experiments.

Ion mobility-mass spectrometry of phosphorylase B ions generated with supercharging reagents but in charge-reducing buffer.

Electrospray ionization high-resolution ion mobility spectrometry-mass spectrometry.

New insights into the vacuum UV photodissociation of peptides.

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166-176

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scholarly article

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10.1039/C5AN01819F

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1

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141

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2015-11-24T00:00:00Z

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4679510

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