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Emerging applications for models of molecular rheology (2008)
Journal Article
Graham, R. S., & McLeish, T. C. (2008). Emerging applications for models of molecular rheology. Journal of Non-Newtonian Fluid Mechanics, 150(1), 11-18. https://doi.org/10.1016/j.jnnfm.2007.09.004

Our understanding of the rich and complex motion of macromolecules has developed rapidly in recent years, particularly in the entangled regime. In this paper we highlight examples of research that has exploited our detailed picture of macromolecular... Read More about Emerging applications for models of molecular rheology.

HyperMacs – long chain hyperbranched polymers: A dramatically improved synthesis and qualitative rheological analysis (2008)
Journal Article
Clarke, N., De Luca, E., Dodds, J., Kimani, S., & Hutchings, L. (2008). HyperMacs – long chain hyperbranched polymers: A dramatically improved synthesis and qualitative rheological analysis. European Polymer Journal, 44(3), 665-676. https://doi.org/10.1016/j.eurpolymj.2007.12.022

We have previously reported a novel (albeit modestly successful) strategy for the synthesis of polystyrene HyperMacs – long chain branched analogues of hyperbranched polymers. The building blocks for HyperMacs, AB2 macromonomers are synthesized by li... Read More about HyperMacs – long chain hyperbranched polymers: A dramatically improved synthesis and qualitative rheological analysis.

Truncation of αB-crystallin by the myopathy-causing Q151X mutation significantly destabilizes the protein leading to aggregate formation in transfected cells (2008)
Journal Article
Hayes, V. H., Devlin, G., & Quinlan, R. A. (2008). Truncation of αB-crystallin by the myopathy-causing Q151X mutation significantly destabilizes the protein leading to aggregate formation in transfected cells. Journal of Biological Chemistry, 283(16), 10500-10512. https://doi.org/10.1074/jbc.m706453200

Here we investigate the effects of a myopathy-causing mutation in αB-crystallin, Q151X, upon its structure and function. This mutation removes the C-terminal domain of αB-crystallin, which is expected to compromise both its oligomerization and chaper... Read More about Truncation of αB-crystallin by the myopathy-causing Q151X mutation significantly destabilizes the protein leading to aggregate formation in transfected cells.

New Dynamical Window onto the Landscape for Forced Protein Unfolding (2008)
Journal Article
Yew, Z., McLeish, T., & Paci, E. (2008). New Dynamical Window onto the Landscape for Forced Protein Unfolding. Physical Review Letters, 101(24), Article 248104. https://doi.org/10.1103/physrevlett.101.248104

The unfolding of a protein by the application of an external force pulling two atoms of the protein can be detected by atomic force and optical tweezers technologies as have been broadly demonstrated in the past decade. Variation of the applied force... Read More about New Dynamical Window onto the Landscape for Forced Protein Unfolding.