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Tandem repeating modular proteins avoid aggregation in single molecule force spectroscopy experiments.

Lorna Dougan1, Julio M Fernandez

  • 1Department of Biological Sciences, Columbia University, New York, New York 10027, USA. ldougan@biology.columbia.edu

The Journal of Physical Chemistry. A
|November 21, 2007
PubMed
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Single molecule force spectroscopy reveals that trifluoroethanol (TFE) does not hinder the refolding of immunoglobulin-like I27 proteins, even at high concentrations. This finding challenges previous observations of protein misfolding in TFE solutions.

Area of Science:

  • Biophysics
  • Protein Folding
  • Biochemistry

Background:

  • Tandem modular proteins with high sequence identity are prone to misfolding and aggregation in aqueous solutions containing cosolvents like trifluoroethanol (TFE).
  • Previous bulk solution experiments indicated that 28% v/v TFE enhances intermolecular attractions, leading to protein misfolding.

Purpose of the Study:

  • To investigate the unfolding and refolding behavior of the immunoglobulin-like I27 protein using single molecule force spectroscopy in aqueous 2,2,2-trifluoroethanol (TFE).
  • To determine if the presence of TFE hinders the refolding of polyproteins with identical repeats.

Main Methods:

  • Single molecule force spectroscopy (SMFS) was employed to probe protein dynamics.
  • A single molecule micromanipulation technique was utilized to analyze the refolding of tandem repeat proteins.

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Main Results:

  • Successful refolding of the polyprotein I27(8) was observed in all tested TFE solutions, up to 35% v/v.
  • Refolding of identical protein repeats was not hindered by the presence of TFE, contrary to expectations from bulk solution studies.

Conclusions:

  • Single molecule experiments provide new insights into the properties of tandem repeating proteins in the presence of cosolvents.
  • The findings raise questions about the evolutionary mechanisms that enable these proteins to avoid misfolding and aggregation.