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@ARTICLE{Strucksberg:60251,
      author       = {Strucksberg, K.H. and Rosenkranz, T. and Fitter, J.},
      title        = {{R}eversible and irreversible unfolding of multi-domain
                      proteins},
      journal      = {Biochimica et biophysica acta / Proteins and proteomics},
      volume       = {1774},
      issn         = {1570-9639},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-60251},
      pages        = {1501 - 1603},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {In contrast to single-domain proteins unfolding of larger
                      multi-domain proteins is often irreversible. In a
                      comparative case study on three different multi-domain
                      proteins (phosphoglycerate kinase: PGK and two homologous
                      alpha-amylases: TAKA and BLA) we investigated properties of
                      unfolded states and their ability to fold back into the
                      native state. For this purpose guanidine hydrochloride,
                      alkaline pH, and thermal unfolded states were characterized.
                      Structural alterations upon unfolding and refolding
                      transitions were monitored using fluorescence and CD
                      spectroscopy. Static and dynamic light scattering was
                      employed to follow aggregation processes. Furthermore,
                      proper refolding was also investigated by enzyme activity
                      measurements. While for PGK at least partial reversible
                      unfolding transitions were observed in most cases, we found
                      reversible unfolding for TAKA in the case of alkaline pH and
                      GndHCl induced unfolding. BLA exhibits reversible unfolding
                      only under conditions with high concentrations of protecting
                      osmolytes (glycerol), indicating that aggregation of the
                      unfolded state is the main obstacle to achieve proper
                      refolding for this protein. Structural properties, such as
                      number and size of domains, secondary structure contents and
                      compositions within domains, and domain topology were
                      analyzed and considered in the interpretation of differences
                      in refolding behavior of the investigated proteins.},
      keywords     = {Aspergillus oryzae: enzymology / Bacillus: enzymology /
                      Buffers / Glycerol: pharmacology / Guanidine: pharmacology /
                      Hydrogen-Ion Concentration / Models, Molecular / Osmolar
                      Concentration / Phosphoglycerate Kinase: chemistry / Protein
                      Denaturation: drug effects / Protein Folding / Protein
                      Structure, Tertiary: drug effects / Protein Structure,
                      Tertiary: physiology / Temperature / Transition Temperature
                      / alpha-Amylases: chemistry / Buffers (NLM Chemicals) /
                      Guanidine (NLM Chemicals) / Glycerol (NLM Chemicals) /
                      Phosphoglycerate Kinase (NLM Chemicals) / alpha-Amylases
                      (NLM Chemicals) / J (WoSType)},
      cin          = {INB-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB805},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17964867},
      UT           = {WOS:000252238600012},
      doi          = {10.1016/j.bbapap.2007.09.005},
      url          = {https://juser.fz-juelich.de/record/60251},
}