@inbook{14847,
  abstract     = {Understanding the mechanisms of chaperones at the atomic level generally requires producing chaperone–client complexes in vitro. This task comes with significant challenges, because one needs to find conditions in which the client protein is presented to the chaperone in a state that binds and at the same time avoid the pitfalls of protein aggregation that are often inherent to such states. The strategy differs significantly for different client proteins and chaperones, but there are common underlying principles. Here, we discuss these principles and deduce the strategies that can be successfully applied for different chaperone–client complexes. We review successful biochemical strategies applied to making the client protein “binding competent” and illustrate the different strategies with examples of recent biophysical and biochemical studies.},
  author       = {Sučec, I. and Schanda, Paul},
  booktitle    = {Biophysics of Molecular Chaperones},
  editor       = {Hiller, Sebastian and Liu, Maili and He, Lichun},
  isbn         = {9781839162824},
  pages        = {136--161},
  publisher    = {Royal Society of Chemistry},
  title        = {{Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies}},
  doi          = {10.1039/bk9781839165986-00136},
  volume       = {29},
  year         = {2023},
}

@inbook{14848,
  abstract     = {Regulating protein states is considered the core function of chaperones. However, despite their importance to all major cellular processes, the conformational changes that chaperones impart on polypeptide chains are difficult to study directly due to their heterogeneous, dynamic, and multi-step nature. Here, we review recent advances towards this aim using single-molecule manipulation methods, which are rapidly revealing new mechanisms of conformational control and helping to define a different perspective on the chaperone function.},
  author       = {Wruck, F. and Avellaneda Sarrió, Mario and Naqvi, M. M. and Koers, E. J. and Till, K. and Gross, L. and Moayed, F. and Roland, A. and Heling, L. W. H. J. and Mashaghi, A. and Tans, S. J.},
  booktitle    = {Biophysics of Molecular Chaperones},
  editor       = {Hiller, Sebastian and Liu, Maili and He, Lichun},
  isbn         = {9781839162824},
  pages        = {278--318},
  publisher    = {Royal Society of Chemistry},
  title        = {{Probing Single Chaperone Substrates}},
  doi          = {10.1039/bk9781839165986-00278},
  volume       = {29},
  year         = {2023},
}