Conformational plasticity of small Hsps (A06)

• Subject Area: Biochemistry
• Term: from 2012 to 2024
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 201302640

Small heat shock proteins (sHsps) are molecular chaperones which act as a first response to proteotoxic stress. A striking feature of sHsps is their existence as dynamic ensembles of interconverting oligomers which is directly linked to their chaperone activity. In previous work, we addressed structural and mechanistic aspects of sHsps including regulatory triggers that control their activity on the conformational level. In future work, we will expand our studies on the conformational dynamics regulating sHsp with a focus on their oligomeric structures, the N terminal region of sHsps and substrate recognition, and mechanistic principles of activity regulation.

• DFG Programme: Collaborative Research Centres
• Subproject of: SFB 1035: Control of Protein Function by Conformational Switching
• Applicant Institution: Technische Universität München (TUM)
• Project Heads: Professor Dr. Johannes Buchner; Dr. Martin Haslbeck, since 7/2016; Professorin Dr. Sevil Weinkauf (†)