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Advances in protein post-translation...

Ni, Wenqin.

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Advances in protein post-translational modifications (PTMS) using liquid chromatography-mass spectrometry.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Advances in protein post-translational modifications (PTMS) using liquid chromatography-mass spectrometry./
Author:	Ni, Wenqin.
Description:	258 p.
Notes:	Source: Dissertation Abstracts International, Volume: 74-07(E), Section: B.
Contained By:	Dissertation Abstracts International74-07B(E).
Subject:	Chemistry, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3556766
ISBN:	9781267990990

Advances in protein post-translational modifications (PTMS) using liquid chromatography-mass spectrometry.
Ni, Wenqin.

Advances in protein post-translational modifications (PTMS) using liquid chromatography-mass spectrometry. - 258 p.

Source: Dissertation Abstracts International, Volume: 74-07(E), Section: B.

Thesis (Ph.D.)--Northeastern University, 2013.

Protein post-translational modifications (PTMs) play significant roles in affecting the physical, chemical, and biological properties of proteins. PTMs can regulate protein functions by modulating protein activity, turnover, cellular location, and protein-protein interaction. In addition, the efficacy and safety of therapeutic protein drugs can be dramatically affected by PTMs. Structural elucidation of complex PTMs provides invaluable insights for the potential roles of PTMs. However, comprehensive characterization of PTMs presents a significant analytical challenge, often requiring the use of multiple orthogonal methods to ensure high confidence in the resulting analytical data. Liquid chromatography coupled with mass spectrometry (LC-MS) is one of the most powerful platforms for determination of PTMs due to its high sensitivity, resolution, and accuracy. LC-MS tools usually can achieve the goal of identification of PTMs, including modified proteins, specific modification sites, and structures of the modifications. This thesis focuses on the methods for the determination of several important PTMs, including deamidation of asparagine, isomerization of aspartic acid, disulfide linkages, and glycosylation using LC-MS approaches.

ISBN: 9781267990990Subjects--Topical Terms:

1021807
Chemistry, General.

Advances in protein post-translational modifications (PTMS) using liquid chromatography-mass spectrometry.
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020 $a 9781267990990
035 $a (MiAaPQ)AAI3556766
035 $a AAI3556766
040 $a MiAaPQ $c MiAaPQ
100 1 $a Ni, Wenqin. $3 2104637
245 1 0 $a Advances in protein post-translational modifications (PTMS) using liquid chromatography-mass spectrometry.
300 $a 258 p.
500 $a Source: Dissertation Abstracts International, Volume: 74-07(E), Section: B.
500 $a Adviser: Barry L. Karger.
502 $a Thesis (Ph.D.)--Northeastern University, 2013.
520 $a Protein post-translational modifications (PTMs) play significant roles in affecting the physical, chemical, and biological properties of proteins. PTMs can regulate protein functions by modulating protein activity, turnover, cellular location, and protein-protein interaction. In addition, the efficacy and safety of therapeutic protein drugs can be dramatically affected by PTMs. Structural elucidation of complex PTMs provides invaluable insights for the potential roles of PTMs. However, comprehensive characterization of PTMs presents a significant analytical challenge, often requiring the use of multiple orthogonal methods to ensure high confidence in the resulting analytical data. Liquid chromatography coupled with mass spectrometry (LC-MS) is one of the most powerful platforms for determination of PTMs due to its high sensitivity, resolution, and accuracy. LC-MS tools usually can achieve the goal of identification of PTMs, including modified proteins, specific modification sites, and structures of the modifications. This thesis focuses on the methods for the determination of several important PTMs, including deamidation of asparagine, isomerization of aspartic acid, disulfide linkages, and glycosylation using LC-MS approaches.
520 $a In chapter 2, a method with differentiation and enrichment of isoaspartic acid (isoAsp) by Asp-N digestion combined with detection and quantification of isoAsp by LC-MS/MS with electron transfer dissociation (ETD) is presented.
520 $a In Chapter 3, a proteome-level analysis of isoAsp in urine proteins from the wild type and protein L-isoaspartyl O-methyltransferase (PIMT, a highly conserved isoAsp repair enzyme) deficient mice is reported.
520 $a In Chapter 4, a successful and robust methodology for complete characterization of disulfide linkages, including cystine knots and nested disulfides in recombinant human arylsulfatase A (rhASA), is developed using multi-enzyme digestion and LC-MS methods with ETD and sequential collision induced dissociation (CID-MS 3) analysis.
520 $a In Chapter 5, the method development for comprehensive characterization of oligosaccharide structures with glycan composition, sequence, linkage, and positional information is described. The newly developed method employs fluoride-mediated negative ionization LC-MS/MS using a microfluidic chip packed with porous graphitized carbon (PGC) for N-glycan separation and an accurate mass quadrupole time of flight (Q-TOF) tandem mass spectrometer for characterization. An application to the characterization of N-glycans released from polyclonal human and murine IgG is described.
590 $a School code: 0160.
650 4 $a Chemistry, General. $3 1021807
650 4 $a Chemistry, Analytical. $3 586156
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0485
690 $a 0486
690 $a 0487
710 2 $a Northeastern University. $b Chemistry & Chemical Biology. $3 2094733
773 0 $t Dissertation Abstracts International $g 74-07B(E).
790 $a 0160
791 $a Ph.D.
792 $a 2013
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3556766