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Single-molecule spectroscopy of unfolded proteins and chaperonin action

  • Hagen Hofmann

    Hagen Hofmann studied Biochemistry at the Martin-Luther University Halle-Wittenberg. During his time as a PhD student in the group of Professor Renate Ulbrich-Hofmann, he used single-molecule fluorescence spectroscopy and NMR-spectroscopy to understand the collapse and folding of the ribonuclease inhibitor barstar. After receiving his PhD, Hagen joined the group of Professor Benjamin Schuler at the University of Zurich where he focuses on the polymeric properties of unfolded and intrinsically disordered proteins and chaperone-mediated protein folding reactions using single-molecule fluorescence spectroscopy.

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Published/Copyright: March 11, 2014
Biological Chemistry
From the journal Biological Chemistry Volume 395 Issue 7-8

Abstract

In the past decade, single-molecule fluorescence techniques provided important insights into the structure and dynamics of proteins. In particular, our understanding of the heterogeneous conformational ensembles of unfolded and intrinsically disordered proteins (IDPs) improved substantially by a combination of FRET-based single-molecule techniques with concepts from polymer physics. A complete knowledge of the forces that act in unfolded polypeptide chains will not only be important to understand the initial steps of protein folding reactions, but it will also be crucial to rationalize the coupling between ligand-binding and folding of IDPs, and the interaction of denatured proteins with molecular chaperones in the crowded cellular environment. Here, I give a personalized review of some of the key findings from my own research that contributed to a more quantitative understanding of unfolded proteins and their interactions with molecular chaperones.

Keywords: IDP; polymer theory; protein collapse; protein folding; scaling laws; single-molecule FRET
Corresponding author: Hagen Hofmann, Department of Biochemistry, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland, e-mail:

About the author

Hagen Hofmann

Hagen Hofmann studied Biochemistry at the Martin-Luther University Halle-Wittenberg. During his time as a PhD student in the group of Professor Renate Ulbrich-Hofmann, he used single-molecule fluorescence spectroscopy and NMR-spectroscopy to understand the collapse and folding of the ribonuclease inhibitor barstar. After receiving his PhD, Hagen joined the group of Professor Benjamin Schuler at the University of Zurich where he focuses on the polymeric properties of unfolded and intrinsically disordered proteins and chaperone-mediated protein folding reactions using single-molecule fluorescence spectroscopy.

Acknowledgments

A part of the described research was initiated while I was a member of the GRK 1026 ‘Conformational transitions in macromolecular interactions,’ which I would like to thank in this particular way for the intellectual and financial support during the wonderful time we had together at the Martin-Luther University Halle-Wittenberg.

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Received: 2014-2-14
Accepted: 2014-3-4
Published Online: 2014-3-11
Published in Print: 2014-7-1

©2014 by Walter de Gruyter Berlin/Boston

Articles in the same Issue

  1. Frontmatter
  2. Guest Editorial
  3. Highlight: conformational transitions in macromolecular interactions
  4. Single-molecule spectroscopy of unfolded proteins and chaperonin action
  5. Influence of the polypeptide environment next to amyloidogenic peptides on fibril formation
  6. Structure of large dsDNA viruses
  7. Functional aspects of extracellular cyclophilins
  8. Generic tools for conditionally altering protein abundance and phenotypes on demand
  9. Structural insights into calmodulin/Munc13 interaction
  10. Interaction of linear polyamines with negatively charged phospholipids: the effect of polyamine charge distance
  11. Interaction of the human N-Ras protein with lipid raft model membranes of varying degrees of complexity
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  13. Insights from reconstitution reactions of COPII vesicle formation using pure components and low mechanical perturbation
  14. Identification of key residues in the formate channel FocA that control import and export of formate
  15. Twin-arginine translocation-arresting protein regions contact TatA and TatB
  16. Biophysical and biochemical analysis of hnRNP K: arginine methylation, reversible aggregation and combinatorial binding to nucleic acids
  17. An ancient oxidoreductase making differential use of its cofactors
  18. Biophysical characterization of polyomavirus minor capsid proteins
  19. Structural basis for PTPA interaction with the invariant C-terminal tail of PP2A
  20. Correlating structure and ligand affinity in drug discovery: a cautionary tale involving second shell residues
  21. Thermodynamic signatures in macromolecular interactions involving conformational flexibility
https://doi.org/10.1515/hsz-2014-0132
Keywords for this article
IDP; polymer theory; protein collapse; protein folding; scaling laws; single-molecule FRET

Articles in the same Issue

  1. Frontmatter
  2. Guest Editorial
  3. Highlight: conformational transitions in macromolecular interactions
  4. Single-molecule spectroscopy of unfolded proteins and chaperonin action
  5. Influence of the polypeptide environment next to amyloidogenic peptides on fibril formation
  6. Structure of large dsDNA viruses
  7. Functional aspects of extracellular cyclophilins
  8. Generic tools for conditionally altering protein abundance and phenotypes on demand
  9. Structural insights into calmodulin/Munc13 interaction
  10. Interaction of linear polyamines with negatively charged phospholipids: the effect of polyamine charge distance
  11. Interaction of the human N-Ras protein with lipid raft model membranes of varying degrees of complexity
  12. Lanthanides as substitutes for calcium ions in the activation of plant α-type phospholipase D
  13. Insights from reconstitution reactions of COPII vesicle formation using pure components and low mechanical perturbation
  14. Identification of key residues in the formate channel FocA that control import and export of formate
  15. Twin-arginine translocation-arresting protein regions contact TatA and TatB
  16. Biophysical and biochemical analysis of hnRNP K: arginine methylation, reversible aggregation and combinatorial binding to nucleic acids
  17. An ancient oxidoreductase making differential use of its cofactors
  18. Biophysical characterization of polyomavirus minor capsid proteins
  19. Structural basis for PTPA interaction with the invariant C-terminal tail of PP2A
  20. Correlating structure and ligand affinity in drug discovery: a cautionary tale involving second shell residues
  21. Thermodynamic signatures in macromolecular interactions involving conformational flexibility
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