Temperature and concentration-controlled dynamics of rhizobial small heat shock proteins.

Journal article

A hallmark of alpha-crystallin-type small heat shock proteins (sHsps) is their highly dynamic oligomeric structure which promotes intermolecular interactions involved in subunit exchange and substrate binding (chaperone-like activity). We studied the oligomeric features of two classes of bacterial sHsps by size exclusion chromatography and nanoelectrospray mass spectrometry. Proteins of both classes formed large complexes that rapidly dissociated upon dilution and at physiologically relevant ...

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Authors: Lentze, N; Aquilina, J; Lindbauer, M; Robinson, C; Narberhaus, F

• Publication status: Published
• Journal: European journal of biochemistry / FEBS
• Volume: 271
• Issue: 12
• Pages: 2494-2503
• Publication date: 2004-06-01
• DOI: 10.1111/j.1432-1033.2004.04180.x
• EISSN: 1432-1033
• ISSN: 0014-2956
• Language: English
• Keywords: Protein Structure, Quaternary; Mass Spectrometry; Models, Molecular; Heat-Shock Proteins; Rhizobium; Chromatography; Molecular Chaperones; Macromolecular Substances; Temperature; Protein Subunits; Circular Dichroism; Protein Structure, Secondary