Grant funding success for the McLain Group

Dr Sylvia McLain has won a grant from The Leverhulme Trust to explore protein folding at the atomic scale.

Image showing representative water-mediated turns in the GPG peptide in solution. (Busch, et al. Angew. Chem. Int. Ed.)

Image showing representative water-mediated turns in the GPG peptide in solution. (Busch, et al. Angew. Chem. Int. Ed.)

The three-year grant will support new work in her group to understand the role of water and urea in the protein folding process. It will boost their recent studies, which have shown that water has an active role in helping proteins attain their folded structure (1,2).

How proteins fold from their linear amino acid sequence into their folded functional forms is not understood. All proteins fold in the presence of at least some water, but water's role in this process remains unclear. Similarly, the mechanism by which small molecules either chaperone proteins to fold, or like urea, disrupt the globular protein structure in aqueous solutions, is even less well understood.

In the project, the group will use a range of experimental and computational approaches to determine the interactions between water and peptides in aqueous solution and how these interactions contribute to protein folding and association. They also hope to understand the specific role that urea plays in unfolding proteins and thereby gain a fuller picture of the folding and unfolding process.

Two new positions are available on the grant - a studentship and a postdoctoral research associate

References

  1. Water mediation essential to nucleation of β-turn formation in peptide folding motifs Angew. Chem., Int Ed., 52 (49), 13091-13095 (2013). Busch, S; Bruce, CD; Redfield C; Lorenz, CD and McLain SE*
    DOI: 10.1002/ange.201307657
  2. Water lends a helping hand in folding

 





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