[go: up one dir, main page]

Craciun, 2008 - Google Patents

Valence Parity Renders z• Type Ions Chemically Distinct

Craciun, 2008

View HTML
Document ID
6899556108875780769
Author
Craciun G
Publication year
Publication venue
Journal of The American Chemical Society

External Links

Snippet

Here we report that the odd electron z•-type ions formed by the electron-based peptide dissociation methods (electron capture or transfer, ECD or ETD) have distinctive chemical compositions from other common product ion types. Specifically, b-, c-, and y-type ions have …
Continue reading at www.academia.edu (HTML) (other versions)

Classifications

    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/68Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
    • G01N33/6803General methods of protein analysis not limited to specific proteins or families of proteins
    • G01N33/6848Methods of protein analysis involving mass spectrometry
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/68Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
    • G01N33/6803General methods of protein analysis not limited to specific proteins or families of proteins
    • G01N33/6842Proteomic analysis of subsets of protein mixtures with reduced complexity, e.g. membrane proteins, phosphoproteins, organelle proteins
    • HELECTRICITY
    • H01BASIC ELECTRIC ELEMENTS
    • H01JELECTRIC DISCHARGE TUBES OR DISCHARGE LAMPS
    • H01J49/00Particle spectrometer or separator tubes
    • H01J49/004Combinations of spectrometers, tandem spectrometers, e.g. MS/MS, MSn
    • H01J49/0045Combinations of spectrometers, tandem spectrometers, e.g. MS/MS, MSn characterised by the fragmentation or other specific reaction
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N30/00Investigating or analysing materials by separation into components using adsorption, absorption or similar phenomena or using ion-exchange, e.g. chromatography or field flow fractionation
    • G01N30/02Column chromatography
    • G01N30/62Detectors specially adapted therefor
    • G01N30/72Mass spectrometers
    • HELECTRICITY
    • H01BASIC ELECTRIC ELEMENTS
    • H01JELECTRIC DISCHARGE TUBES OR DISCHARGE LAMPS
    • H01J49/00Particle spectrometer or separator tubes
    • H01J49/0027Methods for using particle spectrometers
    • H01J49/0036Step by step routines describing the handling of the data generated during a measurement
    • HELECTRICITY
    • H01BASIC ELECTRIC ELEMENTS
    • H01JELECTRIC DISCHARGE TUBES OR DISCHARGE LAMPS
    • H01J49/00Particle spectrometer or separator tubes
    • H01J49/26Mass spectrometers or separator tubes
    • H01J49/34Dynamic spectrometers
    • HELECTRICITY
    • H01BASIC ELECTRIC ELEMENTS
    • H01JELECTRIC DISCHARGE TUBES OR DISCHARGE LAMPS
    • H01J49/00Particle spectrometer or separator tubes
    • H01J49/02Details
    • H01J49/04Arrangements for introducing or extracting samples to be analysed, e.g. vacuum locks; Arrangements for external adjustment of electron- or ion-optical components

Similar Documents

Publication Publication Date Title
Wysocki et al. Mass spectrometry of peptides and proteins
Kind et al. Identification of small molecules using accurate mass MS/MS search
Reid et al. ‘Top down’protein characterization via tandem mass spectrometry
Sztáray et al. Leucine enkephalin—a mass spectrometry standard
Macek et al. Top-down protein sequencing and MS3 on a hybrid linear quadrupole ion trap-orbitrap mass spectrometer
Kellie et al. The emerging process of Top Down mass spectrometry for protein analysis: biomarkers, protein-therapeutics, and achieving high throughput
JP4988884B2 (en) Mass spectrometry system
JP4818270B2 (en) System and method for grouping precursor and fragment ions using selected ion chromatograms
US8592752B2 (en) Techniques for performing retention-time matching of precursor and product ions and for constructing precursor and product ion spectra
JP4515819B2 (en) Mass spectrometry system
US7197402B2 (en) Determination of molecular structures using tandem mass spectrometry
US8530831B1 (en) Probability-based mass spectrometry data acquisition
Heeren et al. A mini-review of mass spectrometry using high-performance FTICR-MS methods
WO2009073505A2 (en) Methods for processing tandem mass spectral data for protein sequence analysis
Majuta et al. Magnifying ion mobility spectrometry–mass spectrometry measurements for biomolecular structure studies
Donohoe et al. Ion mobility spectrometry-hydrogen deuterium exchange mass spectrometry of anions: Part 1. Peptides to proteins
Peterman et al. The use of a hybrid linear trap/FT-ICR mass spectrometer for on-line high resolution/high mass accuracy bottom-up sequencing
Sabareesh et al. Tandem electrospray mass spectrometric studies of proton and sodium ion adducts of neutral peptides with modified N‐and C‐termini: synthetic model peptides and microheterogeneous peptaibol antibiotics
Nagy et al. Optimum collision energies for proteomics: The impact of ion mobility separation
Hubler et al. Valence parity renders z•-type ions chemically distinct
Römpp et al. Examples of Fourier transform ion cyclotron resonance mass spectrometry developments: from ion physics to remote access biochemical mass spectrometry
Huang et al. Top‐down protein characterization facilitated by ion/ion reactions on a quadrupole/time of flight platform
Craciun Valence Parity Renders z• Type Ions Chemically Distinct
Macht Mass spectrometric top-down analysis of proteins
Chalkley Improving peptide identification using empirical scoring systems