FT-ICRMS distinguishes the mechanism of the charge state reduction for multiply charged protein cations admixed with redox reagents in ESI

Journal of Mass Spectrometry

Volumn 41, Issue 5, 2006, Pages 641-645

  Zhao, Cheng ^a   Johnson, Robert W ^b   Bruckenstein, Stanley ^a   Wood, Troy D ^a,c,d  

^a UNIVERSITY AT BUFFALO   (United States)

^b ABBOTT LABORATORIES   (United States)

^c UNIVERSITY AT BUFFALO   (United States)

^d ROSWELL PARK CANCER INSTITUTE   (United States)

Author keywords

Charge reduction; Electrospray ionization; Fourier transform ion cyclotron resonance; Multiply charged; Protein

Indexed keywords

CYCLOTRON RESONANCE; IONIZATION; MASS SPECTROMETRY; OPTICAL RESOLVING POWER; POSITIVE IONS; REDOX REACTIONS; SOLUTION MINING;

CHARGE REDUCTION; ELECTROSPRAY IONIZATION; FOURIER-TRANSFORM ION CYCLOTRON RESONANCE; MULTIPLY CHARGED; PROTON-TRANSFER MECHANISM;

PROTEINS;

1,4 BENZOQUINONE; AMIDE; CATION; PEPTIDE; POLYMACON;

ARTICLE; CIRCULAR DICHROISM; ELECTRON TRANSPORT; FOURIER TRANSFORM MASS SPECTROMETRY; GAS; ION CYCLOTRON RESONANCE MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; PROTON TRANSPORT;

AMIDES; AMINO ACID SEQUENCE; CATIONS; ELECTROCHEMISTRY; FOURIER ANALYSIS; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; PROTEINS; PROTONS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;

EID: 33745774967     PISSN: 10765174     EISSN: 10969888     Source Type: Journal    
DOI: 10.1002/jms.1022     Document Type: Article

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