The dynamics of the proteome: Strategies for measuring protein turnover on a proteome-wide scale (original) (raw)

Journal Article

Heads the Protein Function Group at the University of Liverpool (http://proteomics.liv.ac.uk). His current research interests focus on quantitative proteomics and on the application of proteomics to fundamental studies in animal science. His most cited ‘publication’ (over 300,000 hits!) is a web-based calculator that creates thermodynamically correct buffer recipes (http://www.liv.ac.uk/pfg).

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Received:

21 December 2004

Published:

01 February 2005

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Robert J. Beynon, The dynamics of the proteome: Strategies for measuring protein turnover on a proteome-wide scale, Briefings in Functional Genomics, Volume 3, Issue 4, February 2005, Pages 382–390, https://doi.org/10.1093/bfgp/3.4.382
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Abstract

Quantitative proteomics captures the steady-state amount of a protein in a cell but does not explain how a change in protein amount is manifest — whether through a change in synthesis or a change in degradation. If we are to understand the changes in the proteome, we will need to define such processes. In this brief review, strategies for the determination of intracellular protein dynamics on a proteome-wide scale are discussed.

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© Henry Stewart Publications

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