Jiang Wu
Michigan State University
7 Papers
256 Citations
Jiang Wu is an academic researcher from Michigan State University. The author has contributed to research in topics: Mass spectrometry & Derivatization. The author has an hindex of 7, co-authored 7 publications.
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Papers
A Picomole-Scale Method for Charge Derivatization of Peptides for Sequence Analysis by Mass Spectrometry
TL;DR: Collisionally activated dissociation tandem mass spectrometry of TMPP-Ac-derivatives showed dominant a-type ions, accompanied by d- and c- type ions in some cases, allowing sequence determination to be made in a straightforward manner.
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Protein sequencing by matrix-assisted laser desorption ionization-postsource decay-mass spectrometry analysis of the N-Tris(2,4,6-trimethoxyphenyl)phosphine-acetylated tryptic digests
TL;DR: The TMPP-acetic acid N-hydroxysuccinimide ester is extended now for the direct derivatization of tryptic digests originating from 1-5 microg of proteins with molecular weights from 10-120 kDa, giving rise to product ion spectra that are easily interpretable.
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A Strategy to Locate Cysteine Residues in Proteins by Specific Chemical Cleavage Followed by Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry
TL;DR: This new approach employs a specific reaction between free sulfhydryls and 2-nitro-5-thiocyanobenzoic acid (NTCB) to selectively cyanylate cysteine thiols in peptides and proteins.
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Optimization of the Cleavage Reaction for Cyanylated Cysteinyl Proteins for Efficient and Simplified Mass Mapping
Jiang Wu,J. T. Watson +1 more
TL;DR: The improved cleavage conditions greatly simplify the analytical procedure, which has been successfully applied to the determination of cysteine status in spinach ferredoxin, ovalbumin, and rabbit muscle creatine phosphokinase.
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Trapping of intermediates during the refolding of recombinant human epidermal growth factor (hEGF) by cyanylation, and subsequent structural elucidation by mass spectrometry.
Jiang Wu,Ying Yang,J. T. Watson +2 more
TL;DR: The procedure of quenching and trapping of disulfide intermediates in acidic solution minimizes sulfhydryl‐disulfide exchange, and therefore provides a good measure of folding kinetics and preservation of intermediate species.
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