{"id":175,"date":"2010-03-05T09:28:26","date_gmt":"2010-03-05T14:28:26","guid":{"rendered":"https:\/\/www.bumc.bu.edu\/cbms\/?page_id=175"},"modified":"2019-04-03T18:27:20","modified_gmt":"2019-04-03T22:27:20","slug":"cheng-lin","status":"publish","type":"page","link":"https:\/\/www.bumc.bu.edu\/cbms\/faculty\/cheng-lin\/","title":{"rendered":"Cheng Lin"},"content":{"rendered":"<p><img loading=\"lazy\" width=\"225\" height=\"300\" class=\"alignright wp-image-993 size-medium\" alt=\"Cheng\" src=\"\/cbms\/files\/2010\/03\/Cheng-225x300.jpg\" srcset=\"https:\/\/www.bumc.bu.edu\/cbms\/files\/2010\/03\/Cheng-225x300.jpg 225w, https:\/\/www.bumc.bu.edu\/cbms\/files\/2010\/03\/Cheng-768x1024.jpg 768w, https:\/\/www.bumc.bu.edu\/cbms\/files\/2010\/03\/Cheng.jpg 825w\" sizes=\"(max-width: 225px) 100vw, 225px\" \/>Center for Biomedical Mass Spectrometry<br \/>\nDepartment of Biochemistry<br \/>\nBoston University School of Medicine<br \/>\n670 Albany Street, 5th floor<br \/>\nBoston, MA 02118-2526 USA<\/p>\n<p>Phone: (617)-358-2428<br \/>\nFax:\u00a0\u00a0\u00a0\u00a0\u00a0 (617)-638-6761<br \/>\nEmail: <a href=\"mailto:chenglinATbuDOTedu\">Cheng Lin<\/a><br \/>\n<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/sites\/myncbi\/cheng.lin.1\/bibliography\/40689695\/public\/?sort=date&amp;direction=ascending\">Complete publications<\/a><\/p>\n<p><a href=\"http:\/\/www.bumc.bu.edu\/ftms\/\">Group Site<\/a><\/p>\n<p><strong><em>Research Interests:<\/em><\/strong><\/p>\n<p>A major focus of our current research lies in the development of an integrated approach for high-throughput <em>de novo<\/em> glycan sequencing. We utilize electron activated dissociation (ExD) methods to generate structurally informative tandem mass spectra, both off-line and on-line with various glycan separation methods, including high-performance liquid chromatography (HPLC) and ion mobility spectrometry (IMS), for characterization of complex glycan mixtures. We also carry out theoretical studies to better understand the glycan ExD fragmentation processes, and work with our bioinformatician colleagues to develop software tools for accurate spectral interpretation and\u00a0<em>de novo<\/em> structural determination.<\/p>\n<p>Another key component of our research is the direct MS analysis of protein acylation. Reversible <em>S<\/em>-acylation at cysteine residues modulates the protein hydrophobicity and plays an important regulatory role in protein trafficking, membrane localization and cellular signaling. We are developing sample preparation and LC-MS\/MS methods for enrichment, preservation and reliable characterization of protein acylation.<\/p>\n<p><strong><em>Selected Publications:<\/em><\/strong><\/p>\n<ul>\n<li>Wei, J.; Wu, J.; Tang, Y.; Ridgeway, M.E.; Park, M.A.; Costello, C.E.; Zaia, J.; Lin, C.,\u00a0<em>Characterization and Quantification of Highly Sulfated Glycosaminoglycan Isomers by Gated-Trapped Ion Mobility Spectrometry Negative Electron Transfer Dissociation MS\/MS, Anal. Chem.<\/em>\u00a0<strong>2019<\/strong>,\u00a0<em>91<\/em>, 2994-3001.<\/li>\n<li>Tang, Y.; Wei, J.; Costello, C.E.; Lin, C.,\u00a0<em>Characterization of Isomeric Glycans by Reversed Phase Liquid Chromatography-Electronic Excitation Dissociation Tandem Mass Spectrometry, J. Am. Soc. Mass Spectrom.<\/em>\u00a0<strong>2018<\/strong>,\u00a0<em>90<\/em>, 3793-3801.<\/li>\n<li>Tang, Y.; Pu, Y.; Gao, J.; Hong, P.; Costello, C.E.; Lin, C.,\u00a0<em>De Novo Glycan Sequencing by Electronic Excitation Dissociation and Fixed-Charge Derivatization<\/em>,\u00a0<em>Anal. Chem.<\/em>\u00a0<strong>2018<\/strong>,\u00a0<em>90<\/em>, 3793-3801.<\/li>\n<li>Hong, P.; Sun, H.; Sha, L.; Pu, Y.; Khatri, K.; Yu, X.; Tang, Y.; Lin, C.,\u00a0<em>GlycoDeNovo &#8211; an Efficient Algorithm for Accurate de novo Glycan Topology Reconstruction from Tandem Mass Spectra, J. Am. Soc. Mass Spectrom.<\/em>\u00a0<strong>2017<\/strong>,\u00a0<em>28<\/em>, 2288-2301.<\/li>\n<li>Pu, Y.; Ridgeway, M. E.; Glaskin, R. S.; Park, M. A.; Costello, C. E.; Lin, C., <em>Separation and Identification of Isomeric Glycans by Selected Accumulation-Trapped Ion Mobility Spectrometry-Electron Activated Dissociation Tandem Mass Spectrometry<\/em>, <em>Anal. Chem.<\/em> <strong>2016<\/strong>, <em>88 (7)<\/em>, 3440-3443.<\/li>\n<li>Ji, Y.; Bachschmid, M. M.; Costello, C. E.; Lin, C., <em>S- to N-Palmitoyl Transfer during Proteomic Sample Preparation<\/em>, <em>J. Am. Soc. Mass Spectrom.<\/em> <strong>2016<\/strong>, <em>27 (4)<\/em>, 677-685.<\/li>\n<li>Huang, Y.; Pu, Y.; Yu, X.; Costello, C. E.; Lin, C., <em>Mechanistic Study on Electronic Excitation Dissociation of the Cellobiose-Na<sup>+<\/sup> Complex<\/em>, <em>J. Am. Soc. Mass Spectrom.<\/em> <strong>2016<\/strong>, <em>27<\/em>, 319-328.<\/li>\n<li>Yu, X.; Sargaeva, N. P.; Thompson, C. J.; Costello, C. E.; Lin, C., <em>In-Source Decay Characterization of Isoaspartate and <\/em><em>\u03b2-Peptides<\/em>, <em>Int. J. Mass Spectrom. <\/em><strong>2015<\/strong>, <em>390<\/em>, 101-109.<\/li>\n<li>Ji, Y.; Liu, M.; Bachschmid, M. M.; Costello, C. E.; Lin, C., <em>Surfactant-Induced Artifacts during Proteomics Sample Preparation<\/em><em>, <\/em><em>Anal. Chem.<\/em> <strong>2015<\/strong>, <em>87 (11)<\/em>, 5500-5504.<\/li>\n<li>Huang, Y.; Pu, Y.; Yu, X.; Costello, C. E.; Lin, C., <em>Mechanistic Study on Electron Capture Dissociation of the Oligosaccharide-Mg<sup>2+<\/sup> Complex<\/em><em>, J. Am. Soc. Mass Spectrom. <strong>2014<\/strong>, <em>25<\/em>, 1451-1460.<\/em><\/li>\n<li>Ji, Y.; Leymarie, N.; Haeussler, D. J.; Bachschmid, M. M.; Costello, C. E.; Lin, C., <em>Direct Detection of S-Palmitoylation by Mass Spectrometry<\/em><em>, Anal. Chem. <strong>2013<\/strong>, <em>85 (24)<\/em>, 11952-11959.<\/em><\/li>\n<li>Yu, X.; Jiang, Y.; Chen, Y.; Huang, Y.; Costello, C. E.; Lin, C., <em>Detailed Glycan Structural Characterization by Electronic Excitation Dissociation<\/em>, <em>Anal. Chem.<\/em> <strong>2013<\/strong>, <em>85 (21)<\/em>, 10017-10021.<\/li>\n<li>Huang, Y.; Yu, X.; Mao, Y.; Costello, C. E.; Zaia, J.; Lin, C., <em>De Novo Sequencing of Heparan Sulfate Oligosaccharides by Electron-Activated Dissociation<\/em><em>, Anal. Chem. <strong>2013<\/strong>, <em>85 (24)<\/em>, 11979-11986.<\/em><\/li>\n<li>Li, X.; Yu, X.; Costello, C. E.; Lin, C.; O&#8217;Connor, P. B., <em>Top-Down Study of \u03b22-Microglobulin Deamidation, Anal. Chem. <strong>2012<\/strong>, <em>84 (14)<\/em>, 6150-6157.<\/em><\/li>\n<li>Yu, X.; Huang, Y.; Lin, C.; Costello, C. E., <em>Energy-Dependent Electron Activated Dissociation of Metal-Adducted Permethylated Oligosaccharides<\/em>, <em>Anal. Chem.<\/em> <strong>2012<\/strong>, <em>84 (12)<\/em>, 7487-7494.<\/li>\n<li>Li, X.; Huang, Y.; O&#8217;Connor, P. B.; Lin, C., <em>Structural Heterogeneity of Doubly-Charged Peptide b-Ions<\/em>, <em>J. Am. Soc. Mass Spectrom.<\/em> <strong>2011<\/strong>, <em>22<\/em>, 245-254.<\/li>\n<li>Sargaeva, N. P.; Lin, C.; O\u2019Connor, P. B., <em>Identification of Aspartic and Isoaspartic Acid Residues in Amyloid \u03b2 Peptides, Including A\u03b21\u221242, Using Electron\u2212Ion Reactions<\/em>, <em>Anal. Chem<\/em>. <strong>2009<\/strong>, <em>81<\/em>, 9778-9786.<\/li>\n<li>Lin, C.; Cournoyer, J. J.; O\u2019Connor, P. B., <em>Probing the Gas Phase Folding Kinetics of Peptide Ions by IR Activated DR-ECD<\/em>, <em>J. Am. Soc. Mass Spectrom<\/em>. <strong>2008<\/strong>, <em>19<\/em>, 780.<\/li>\n<li>Lin, C.; Mathur, R.; Aizikov, K.; O\u2019Connor, P. B., <em>First Signal on the Cryogenic Fourier-Transform Ion Cyclotron Resonance Mass Spectrometer<\/em>, <em>J. Am. Soc. Mass Spectrom<\/em>. <strong>2007<\/strong>, <em>18<\/em>, 2090.<\/li>\n<li>Lin, C.; Cournoyer, J. J.; O\u2019Connor, P. B., <em>Use of a Double Resonance Electron Capture Dissociation Experiment to Probe Fragment Intermediate Lifetimes<\/em>, <em>J. Am. Soc. Mass Spectrom<\/em>. <strong>2006<\/strong>, <em>17<\/em>, 1605.<\/li>\n<li>Cournoyer, J. J.; Lin, C.; O\u2019Connor, P. B., <em>Detecting Deamidation Products in Proteins by Electron Capture Dissociation<\/em>,\u00a0 <em>Anal. Chem<\/em>. <strong>2006<\/strong>, <em>78<\/em>, 1264.<\/li>\n<li>Oh, H.-B.; Lin, C.; Hwang, H. Y.; Zhai, H.; Breuker, K.; Zabrouskov, V.; Carpenter, B. K.; McLafferty, F. W., <em>Infrared Photodissociation Spectroscopy of Electrosprayed Ions in a Fourier-Transform Mass Spectrometer,<\/em>\u00a0<em>J. Am. Chem. Soc<\/em>. <strong>2005<\/strong>, <em>127<\/em>, 4076.<\/li>\n<li>Breuker, K.; Oh, H.-B.; Lin, C.; Carpenter, B. K.; McLafferty, F. W., <em>Nonergodic and Conformational Control of the Electron Capture Dissociation of Protein Cations<\/em>,\u00a0 <em>Proc. Nat. Acad. Sci. USA<\/em> <strong>2004<\/strong>, <em>101<\/em>, 14011.<\/li>\n<li>Lin, C.; Witinski, M. F.; Davis, H. F.,\u00a0<em>Oxygen Atom Rydberg Time-of-Flight Spectroscopy<\/em>, <em>J. Chem. Phys.<\/em> <strong>2003<\/strong>, <em>119<\/em>, 251.<\/li>\n<li>Strazisar, B. R.; Lin, C.; Davis, H. F., <em>Vibrationally Inelastic Scattering of High-n Rydberg H Atoms from N2 and O2<\/em>, <em>Phys. Rev. Lett.<\/em> <strong>2001<\/strong>, <em>86<\/em>, 3997.<\/li>\n<li>Strazisar, B. R.; Lin, C.; Davis, H. F., <em>Mode Specific Energy Disposal in the 4-Atom Reaction OH + D2 -&gt; HOD + D<\/em>,\u00a0<em>Science<\/em> <strong>2000<\/strong>, <em>290<\/em>, 958.<\/li>\n<\/ul>\n","protected":false},"excerpt":{"rendered":"<p>Center for Biomedical Mass Spectrometry Department of Biochemistry Boston University School of Medicine 670 Albany Street, 5th floor Boston, MA 02118-2526 USA Phone: (617)-358-2428 Fax:\u00a0\u00a0\u00a0\u00a0\u00a0 (617)-638-6761 Email: Cheng Lin Complete publications Group Site Research Interests: A major focus of our current research lies in the development of an integrated approach for high-throughput de novo glycan [&hellip;]<\/p>\n","protected":false},"author":1067,"featured_media":0,"parent":7,"menu_order":2,"comment_status":"closed","ping_status":"closed","template":"","meta":[],"_links":{"self":[{"href":"https:\/\/www.bumc.bu.edu\/cbms\/wp-json\/wp\/v2\/pages\/175"}],"collection":[{"href":"https:\/\/www.bumc.bu.edu\/cbms\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/www.bumc.bu.edu\/cbms\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/www.bumc.bu.edu\/cbms\/wp-json\/wp\/v2\/users\/1067"}],"replies":[{"embeddable":true,"href":"https:\/\/www.bumc.bu.edu\/cbms\/wp-json\/wp\/v2\/comments?post=175"}],"version-history":[{"count":25,"href":"https:\/\/www.bumc.bu.edu\/cbms\/wp-json\/wp\/v2\/pages\/175\/revisions"}],"predecessor-version":[{"id":1190,"href":"https:\/\/www.bumc.bu.edu\/cbms\/wp-json\/wp\/v2\/pages\/175\/revisions\/1190"}],"up":[{"embeddable":true,"href":"https:\/\/www.bumc.bu.edu\/cbms\/wp-json\/wp\/v2\/pages\/7"}],"wp:attachment":[{"href":"https:\/\/www.bumc.bu.edu\/cbms\/wp-json\/wp\/v2\/media?parent=175"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}