Mapping native disulfide bonds at a proteome scale
Nature methods, 2015•nature.com
We developed a high-throughput mass spectrometry method, pLink-SS (http://pfind. ict. ac.
cn/software/pLink/2014/pLink-SS. html), for precise identification of disulfide-linked peptides.
Using pLink-SS, we mapped all native disulfide bonds of a monoclonal antibody and ten
standard proteins. We performed disulfide proteome analyses and identified 199 disulfide
bonds in Escherichia coli and 568 in proteins secreted by human endothelial cells. We
discovered many regulatory disulfide bonds involving catalytic or metal-binding cysteine …
cn/software/pLink/2014/pLink-SS. html), for precise identification of disulfide-linked peptides.
Using pLink-SS, we mapped all native disulfide bonds of a monoclonal antibody and ten
standard proteins. We performed disulfide proteome analyses and identified 199 disulfide
bonds in Escherichia coli and 568 in proteins secreted by human endothelial cells. We
discovered many regulatory disulfide bonds involving catalytic or metal-binding cysteine …
Abstract
We developed a high-throughput mass spectrometry method, pLink-SS (http://pfind.ict.ac.cn/software/pLink/2014/pLink-SS.html), for precise identification of disulfide-linked peptides. Using pLink-SS, we mapped all native disulfide bonds of a monoclonal antibody and ten standard proteins. We performed disulfide proteome analyses and identified 199 disulfide bonds in Escherichia coli and 568 in proteins secreted by human endothelial cells. We discovered many regulatory disulfide bonds involving catalytic or metal-binding cysteine residues.
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