Optimization of mass spectrometry-compatible surfactants for shotgun proteomics.

Optimization of mass spectrometry-compatible surfactants for shotgun proteomics. Research Abstract Details 

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Optimization of mass spectrometry-compatible surfactants for shotgun proteomics. Abstract Text:

Emily I Chen,Daniel Cociorva,Jeremy L Norris,John R Yates,

An optimization and comparison of trypsin digestion strategies for peptide/protein identifications by microLC-MS/MS with or without MS compatible detergents in mixed organic-aqueous and aqueous systems was carried out in this study. We determine that adding MS-compatible detergents to proteolytic digestion protocols dramatically increases peptide and protein identifications in complex protein mixtures by shotgun proteomics. Protein solubilization and proteolytic efficiency are increased by including MS-compatible detergents in trypsin digestion buffers. A modified trypsin digestion protocol incorporating the MS compatible detergents consistently identifies over 300 proteins from 5 microg of pancreatic cell lysates and generates a greater number of peptide identifications than trypsin digestion with urea when using LC-MS/MS. Furthermore, over 700 proteins were identified by merging protein identifications from trypsin digestion with three different MS-compatible detergents. We also observe that the use of mixed aqueous and organic solvent systems can influence protein identifications in combinations with different MS-compatible detergents. Peptide mixtures generated from different MS-compatible detergents and buffer combinations show a significant difference in hydrophobicity. Our results show that protein digestion schemes incorporating MS-compatible detergents generate quantitative as well as qualitative changes in observed peptide identifications, which lead to increased protein identifications overall and potentially increased identification of low-abundance proteins.

Optimization of mass spectrometry-compatible surfactants for shotgun proteomics. Publishing Authors By Initials

EI Chen,D Cociorva,JL Norris,JR Yates,

For similar enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: serine endopeptidases: trypsin research abstracts see: enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: serine endopeptidases: trypsin research

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Optimization of mass spectrometry-compatible surfactants for shotgun proteomics. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Journal of proteome research

VOLUME: 6

Page Numbers: 2529-38

Journal Abbreviation: J. Proteome Res.

ISSN: 1535-3893

DAY: 27

MONTH: 05

YEAR: 2007

Optimization of mass spectrometry-compatible surfactants for shotgun proteomics. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 101128775

Optimization of mass spectrometry-compatible surfactants for shotgun proteomics. Keywords Mesh Terms:

KEYWORDS: Trypsin

MESH TERMS: chemistry

Chemical & Substance for Abstract: Optimization of mass spectrometry-compatible surfactants for shotgun proteomics. Information

Substance Name: Trypsin

Registry Number: EC 3.4.21.4

Grant and Affiliation Information for Optimization of mass spectrometry-compatible surfactants for shotgun proteomics.

AFFILIATION: Department of Cell Biology, 10550 North Torrey Pines Road, SR11, The Scripps Research Institute, La Jolla, California 92037, USA.

Country: United States

AGENCY: United States PHS

GRANT: UCSD/MCB0237059

ACRONYM: RR

MEDLINETA: J Proteome Res

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