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Best practices and benchmarks for intact protein analysis for top-down mass spectrometry.

Authors :
Donnelly, Daniel P
Donnelly, Daniel P
Rawlins, Catherine M
DeHart, Caroline J
Fornelli, Luca
Schachner, Luis F
Lin, Ziqing
Lippens, Jennifer L
Aluri, Krishna C
Sarin, Richa
Chen, Bifan
Lantz, Carter
Jung, Wonhyeuk
Johnson, Kendall R
Koller, Antonius
Wolff, Jeremy J
Campuzano, Iain DG
Auclair, Jared R
Ivanov, Alexander R
Whitelegge, Julian P
Paša-Tolić, Ljiljana
Chamot-Rooke, Julia
Danis, Paul O
Smith, Lloyd M
Tsybin, Yury O
Loo, Joseph A
Ge, Ying
Kelleher, Neil L
Agar, Jeffrey N
Donnelly, Daniel P
Donnelly, Daniel P
Rawlins, Catherine M
DeHart, Caroline J
Fornelli, Luca
Schachner, Luis F
Lin, Ziqing
Lippens, Jennifer L
Aluri, Krishna C
Sarin, Richa
Chen, Bifan
Lantz, Carter
Jung, Wonhyeuk
Johnson, Kendall R
Koller, Antonius
Wolff, Jeremy J
Campuzano, Iain DG
Auclair, Jared R
Ivanov, Alexander R
Whitelegge, Julian P
Paša-Tolić, Ljiljana
Chamot-Rooke, Julia
Danis, Paul O
Smith, Lloyd M
Tsybin, Yury O
Loo, Joseph A
Ge, Ying
Kelleher, Neil L
Agar, Jeffrey N
Source :
Nature methods; vol 16, iss 7, 587-594; 1548-7091
Publication Year :
2019

Abstract

One gene can give rise to many functionally distinct proteoforms, each of which has a characteristic molecular mass. Top-down mass spectrometry enables the analysis of intact proteins and proteoforms. Here members of the Consortium for Top-Down Proteomics provide a decision tree that guides researchers to robust protocols for mass analysis of intact proteins (antibodies, membrane proteins and others) from mixtures of varying complexity. We also present cross-platform analytical benchmarks using a protein standard sample, to allow users to gauge their proficiency.

Details

Database :
OAIster
Journal :
Nature methods; vol 16, iss 7, 587-594; 1548-7091
Notes :
application/pdf, Nature methods vol 16, iss 7, 587-594 1548-7091
Publication Type :
Electronic Resource
Accession number :
edsoai.on1287397907
Document Type :
Electronic Resource