Introduction to protein mass spectrometry

Ismael Cotte-Rodriguez; Zhixin Miao; Yun Zhang; Hao Chen

doi:10.1007/978-1-4419-7862-2_1

Introduction to protein mass spectrometry

Ismael Cotte-Rodriguez, Zhixin Miao, Yun Zhang, Hao Chen

Research output: Chapter in Book/Report/Conference proceeding › Chapter

Abstract

Proteins fulfill a plethora of biochemical functions within every living organism, and mass spectrometry (MS) has become one of the most powerful and popular modern physical-chemical methods to study the complexities of proteins. In particular, the invention of matrix-assisted laser desorption/ionization (MALDI) [1] and electrospray ionization (ESI) technologies[2, 3] allows one to measure protein molecular weights and sequences, and to probe conformations and post-translational modifications of proteins. In addition, the mass range of species amenable for MS analysis has increased, enabling the transfer of ionized non-covalent species with masses well over one million (e.g., 1.5 MDa 24-Mer flavoprotein vanillyl-alcohol oxidase (VAO) from Penicillium simplicissimum [4]) into the gas phase. These advances moved MS into the range of intact protein oligomers and functional machineries.

Original language	English (US)
Title of host publication	Characterization of Protein Therapeutics using Mass Spectrometry
Publisher	Springer US
Pages	1-58
Number of pages	58
Volume	9781441978622
ISBN (Electronic)	9781441978622
ISBN (Print)	1441978615, 9781441978615
DOIs	https://doi.org/10.1007/978-1-4419-7862-2_1
State	Published - Oct 1 2013
Externally published	Yes

All Science Journal Classification (ASJC) codes

General Chemistry

Access to Document

10.1007/978-1-4419-7862-2_1

Cite this

@inbook{6135d0f22a2043ecaa424d602b3d8cdd,

title = "Introduction to protein mass spectrometry",

abstract = "Proteins fulfill a plethora of biochemical functions within every living organism, and mass spectrometry (MS) has become one of the most powerful and popular modern physical-chemical methods to study the complexities of proteins. In particular, the invention of matrix-assisted laser desorption/ionization (MALDI) [1] and electrospray ionization (ESI) technologies[2, 3] allows one to measure protein molecular weights and sequences, and to probe conformations and post-translational modifications of proteins. In addition, the mass range of species amenable for MS analysis has increased, enabling the transfer of ionized non-covalent species with masses well over one million (e.g., 1.5 MDa 24-Mer flavoprotein vanillyl-alcohol oxidase (VAO) from Penicillium simplicissimum [4]) into the gas phase. These advances moved MS into the range of intact protein oligomers and functional machineries.",

author = "Ismael Cotte-Rodriguez and Zhixin Miao and Yun Zhang and Hao Chen",

note = "Publisher Copyright: {\textcopyright} 2013 Springer Science+Business Media New York. All rights are reserved.",

year = "2013",

month = oct,

day = "1",

doi = "10.1007/978-1-4419-7862-2_1",

language = "English (US)",

isbn = "1441978615",

volume = "9781441978622",

pages = "1--58",

booktitle = "Characterization of Protein Therapeutics using Mass Spectrometry",

publisher = "Springer US",

address = "United States",

}

TY - CHAP

T1 - Introduction to protein mass spectrometry

AU - Cotte-Rodriguez, Ismael

AU - Miao, Zhixin

AU - Zhang, Yun

AU - Chen, Hao

PY - 2013/10/1

Y1 - 2013/10/1

N2 - Proteins fulfill a plethora of biochemical functions within every living organism, and mass spectrometry (MS) has become one of the most powerful and popular modern physical-chemical methods to study the complexities of proteins. In particular, the invention of matrix-assisted laser desorption/ionization (MALDI) [1] and electrospray ionization (ESI) technologies[2, 3] allows one to measure protein molecular weights and sequences, and to probe conformations and post-translational modifications of proteins. In addition, the mass range of species amenable for MS analysis has increased, enabling the transfer of ionized non-covalent species with masses well over one million (e.g., 1.5 MDa 24-Mer flavoprotein vanillyl-alcohol oxidase (VAO) from Penicillium simplicissimum [4]) into the gas phase. These advances moved MS into the range of intact protein oligomers and functional machineries.

AB - Proteins fulfill a plethora of biochemical functions within every living organism, and mass spectrometry (MS) has become one of the most powerful and popular modern physical-chemical methods to study the complexities of proteins. In particular, the invention of matrix-assisted laser desorption/ionization (MALDI) [1] and electrospray ionization (ESI) technologies[2, 3] allows one to measure protein molecular weights and sequences, and to probe conformations and post-translational modifications of proteins. In addition, the mass range of species amenable for MS analysis has increased, enabling the transfer of ionized non-covalent species with masses well over one million (e.g., 1.5 MDa 24-Mer flavoprotein vanillyl-alcohol oxidase (VAO) from Penicillium simplicissimum [4]) into the gas phase. These advances moved MS into the range of intact protein oligomers and functional machineries.

UR - http://www.scopus.com/inward/record.url?scp=84949177640&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84949177640&partnerID=8YFLogxK

U2 - 10.1007/978-1-4419-7862-2_1

DO - 10.1007/978-1-4419-7862-2_1

M3 - Chapter

AN - SCOPUS:84949177640

SN - 1441978615

SN - 9781441978615

VL - 9781441978622

SP - 1

EP - 58

BT - Characterization of Protein Therapeutics using Mass Spectrometry

PB - Springer US

ER -

Introduction to protein mass spectrometry

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this