Protein structure, function and interactions

We use a variety of spectroscopic, biophysical and protein chemical techniques to study molecular chaperone proteins and their mechanism of stabilising other proteins, for example those involved in diseases of protein aggregation (Alzheimer’s, Parkinson’s, cataract etc.). NMR spectroscopy is the principal technique used to characterise these interactions. 


  • G.K.A. Hochberg, H. Ecroyd, C. Liu, D. Cox, D. Cascio, M.R. Sawaya, M.P. Collier, J. Stroud, J.A. Carver, A.J. Baldwin, C.V. Robinson, D. Eisenberg, J.L.P. Benesch and A. Laganowsky. A structured core domain of aB-crystallin can prevent amyloid fibrillation and associated toxicity. Proc. Natl. Acad. Sci. USA 111, E1562-1570 (2014).
  • G. Esposito, M. Garvey, V. Alverdi, F. Pettirossi, A. Corazza, F. Fogolari, M. Polano, P.P. Mangione, S. Giorgetti, M. Stoppini, A. Rekas, V. Bellotti, A.J.R. Heck and J.A. Carver. Monitoring the interaction between b2-microglobulin and the molecular chaperone aB-crystallin by NMR and mass spectrometry. aB-Crystallin dissociates b2-microglobulin oligomers. J. Biol. Chem. 288, 17844-17858 (2013).
  • C. Holt, J.A. Carver, H. Ecroyd and D.C. Thorn. Caseins and the casein micelle: their biological functions, structures and behavior in foods. J. Dairy Sci. 96, 6127-6146 (2013).
  • C. Holt and J.A. Carver. Darwinian transformation of a ‘scarcely nutritious fluid’ into milk. J. Evol. Biol. 25, 1253-1263 (2012).
  • S.L. Shammas, C.A. Waudby, S. Wang, A.K. Buell, H. Ecroyd, M.E. Welland, J.A. Carver, C.M. Dobson and S. Meehan. Binding of the molecular chaperone aB-crystallin to Ab amyloid fibrils inhibits elongation. Biophys. J. 101, 1681-1689 (2011).
  • D.M. Williams, H. Ecroyd, K.L. Goodwin, H. Dai, H. Fu, J.M. Woodcock, L. Zhang and J.A. Carver. NMR spectroscopy of 14-3-3z reveals a flexible C-terminal extension. Differentiation of the chaperone and phosphoserine binding affinities of 14-3-3z. Biochem. J. 437, 493-503 (2011).
  • A.L. Robertson, S.J. Headey, H.M. Saunders, H. Ecroyd, M.J. Scanlon, J.A. Carver and S.P. Bottomley. Small heat-shock proteins inhibit polyglutamine aggregation by interactions with a flanking domain. Proc. Natl. Acad. Sci. USA 107, 10424-10429 (2010).
  • S.A. Hudson, H. Ecroyd, T.W. Kee and J.A. Carver. The thioflavin T fluorescence assay for amyloid fibril detection is biased by the presence of chromophoric compounds. FEBS J. 276, 5960-5972 (2009).
  • H. Ecroyd and J.A. Carver. Crystallin proteins and amyloid fibrils. Cell. Mol. Life Sci. 66, 62-81 (2009).
  • S. Meehan, T.P. Knowles, A.J. Baldwin, J.F. Smith, A.M. Squires, P. Clements, T.M. Treweek, H. Ecroyd, G.G. Tartaglia, M, Vendruscolo, C.E. MacPhee, C.M. Dobson and J.A. Carver. Characterisation of amyloid fibril formation by small heat-shock chaperone proteins, human aA-, aB- and R120G aB-crystallins. J. Mol. Biol. 372, 470-484 (2007).
  • H. Ecroyd, S. Meehan, J. Horwitz, J.A. Aquilina, J.L.P. Benesch, C.V. Robinson, C.E. MacPhee and J.A. Carver. Mimicking phosphorylation of aB-crystallin affects its chaperone activity. Biochem. J. 401, 129-141 (2007).
  • D.C. Thorn, S. Meehan, M. Sunde, A. Rekas, S.L. Gras, C.E. MacPhee, C.M. Dobson, M.R. Wilson and J.A. Carver. Amyloid fibril formation by bovine milk k-casein and its inhibition by the molecular chaperones as- and b-casein. Biochemistry 44, 17027-17036 (2005).

Updated:  28 March 2017/Responsible Officer:  Director, RSC/Page Contact:  Web Admin, RSC