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αB-crystallin polydispersity is a consequence of unbiased quaternary dynamics.

Abstract:

The inherent heterogeneity of many protein assemblies complicates characterization of their structure and dynamics, as most biophysical techniques require homogeneous preparations of isolated components. For this reason, quantitative studies of the molecular chaperone αB-crystallin, which populates a range of interconverting oligomeric states, have been difficult, and the physicochemical basis for its polydispersity has remained unknown. Here, we perform mass spectrometry experiments to study...

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2011.07.016

Authors


Journal:
Journal of molecular biology
Volume:
413
Issue:
2
Pages:
297-309
Publication date:
2011-10-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:f70de3ba-62f0-46ca-96d9-5bd9002a085b
Source identifiers:
170181
Local pid:
pubs:170181

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