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2015 | 2 | 1 |

Article title

Stabilization of the “open” conformer of apoIscU
on the surface of polystyrene nanobeads
accelerates assembly of a 2Fe2S structure


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The scaffold protein IscU is involved in the
assembly/transfer of FeS clusters. IscU exists in both
open and closed conformation. The clusterless open
conformation of IscU adheres to the hydrophobic
surface of polystyrene nanobeads, as observed for other
proteins. Increased accessibility of the ligand cysteines
in bound IscU facilitates assembly of a 2Fe2S cluster,
and the cluster-bearing structured form of IscU does not
interact with the nanobeads, thus ensuring turnover.
The dependence of accelerated cluster assembly on the
nanobeads concentration pointed to steric and crowding
effects as for promoting cluster formation, and confirms
the requirement for structural flexibility of IscU .









Physical description


13 - 7 - 2015
20 - 1 - 2016
27 - 9 - 2015


  • Section of
    Chemical and Biomolecular Sciences, DeFENS, University of Milan
  • Section of
    Chemical and Biomolecular Sciences, DeFENS, University of Milan
  • DeFENS, University of
    Milan, Via Celoria 2, 20133, Milan, Italy
  • Section of
    Chemical and Biomolecular Sciences, DeFENS, University of Milan


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