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A quantitative strategy to detect changes in accessibility of protein regions to chemical modification on heterodimerization.

Abstract:

We describe a method for studying quantitative changes in accessibility of surface lysine residues of the PB1 subunit of the influenza RNA polymerase as a result of association with the PA subunit to form a PB1-PA heterodimer. Our method combines two established methods: (i) the chemical modification of surface lysine residues of native proteins by N-hydroxysuccinimidobiotin (NHS-biotin) and (ii) the stable isotope labeling of amino acids in cell culture (SILAC) followed by tryptic digestion ...

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Publication status:
Published

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Publisher copy:
10.1002/pro.159

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Institution:
University of Oxford
Department:
Oxford, MSD, Pathology Dunn School
Journal:
Protein science : a publication of the Protein Society
Volume:
18
Issue:
7
Pages:
1448-1458
Publication date:
2009-07-05
DOI:
EISSN:
1469-896X
ISSN:
0961-8368
URN:
uuid:b91c0448-e956-4596-829e-66c06694e016
Source identifiers:
259
Local pid:
pubs:259

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