研究领域

Physical chemistry

Our research focuses on using biomolecular NMR techniques to study the biophysical basis of function, and malfunction, of proteins in health and disease. We combine advanced solution and solids NMR spectroscopy techniques with complementary methods such as ion-mobility mass spectrometry and electron microscopy in order to study the structure and dynamics of proteins, and relate this to their behaviour in the cell.

近期论文

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Collision Cross Sections for Structural Proteomics Maryland EG, Degiacomi MT, Robinson CV, Baldwin AJ, Benesch JLP Structure (2015) in press Combining tandem mass spectrometry with ion mobility separation to determine the architecture of polydisperse proteins Shepherd DA, Marty MT, Giles K, Baldwin AJ, Benesch JLP Int. J mass spec. (2015) in press Phase transition of a disordered Nuage protein generates environmentally responsive membraneless organelles Nott TJ, Petsalaki E, Farber P, Jervis D, Fussner E, Plochowietz A, Craggs T, Bazett-Jones DP, Forman-Kay JP, Baldwin AJ, PawsonT Molecular Cell (2015) 57 936-947 Membrane proteins bind lipids selectively to modulate their structure and function Laganowsky A, Reading E, Allison T, Ulmschneider MB, Degiacomi MT, Baldwin AJ, Robinson CV Nature (2014), 510 7503, 172-175 The structured core domain of αB-crystallin can prevent amyloid fibrillation and associated toxicity Hochberg GKA, Ecroyd H, Liu C, Cox D, Csciod D, Sawaya MR, Colliera MP, Stroud J, Carver JA, Baldwin AJ, Robinson CV, Eisenberg DS, Benesch JLP, Laganowsky A PNAS (2014) 111, E1562-70 An exact solution for R2,eff in CPMG experiments in the case of two site chemical exchange Baldwin AJ JMR (2014), 244, 114-124 An R1ρ expression for a spin in chemical exchange between two sites with unequal transverse relaxation rates Baldwin AJ, Kay LE J. Biol. NMR (2013), 55:211-218 C-terminal Interactions Mediate the Quaternary Dynamics of αB-crystallin Hilton GR, Hochberg GKA, Laganowsky A, McGinnigle SI, Baldwin AJ, Benesch JLP Phil. Trans. R. Soc. B. (2013) 368 20110405 Small heat-Shock proteins: paramedics of the cell Hilton GR, Lioe H, Stengel F, Baldwin AJ, Benesch JLP Top. Curr. Chem. (2013) 328:69-98 Twisting Transition between Crystalline and Fibrillar Phases of Aggregated Peptides Knowles TPJ, Simone AD, Fitzpatrick AW, Baldwin AJ, Meehan S, Rajah L, Vendruscolo M, Welland ME, Dobson CM, Terentjev EM PRL (2012) 109(15) 15101 Dynamic binding Baldwin AJ, Kay LE Nature (2012) 488(7410): 165-6 Probing dynamic conformations of the high molecular weight αB-crystallin heat shock protein ensemble by NMR spectroscopy Baldwin AJ, Walsh P, Hansen DF, Hilton GR, Benesch JLP, Sharpe S, Kay LE J. Am. Chem. Soc. (2012) 134(37) 15343-50 Dissecting heterogeneous molecular chaperone complexes using a mass spectrum deconvolution approach Baldwin AJ*, Stengel F*, Bush MF, Hilton GR, Lioe H, Basha E, Jaya N, Vierling E, Benesch JLP Chem & Biol. (2012) 19: 599-607 Measurement of the signs of methyl chemical shift differences between ground and excited protein states by R1ρ: an application to αB-crystallin Baldwin AJ, Kay LE J. Biol. NMR (2012) 53(1): 1 The morphology of decorated amyloid fibers is controlled by the conformation and position of the displayed protein Forman CJ, Nickson AA, Anthony-Cahill SJ, Baldwin AJ, Kaggwa G, Feber U, Sheikh K, Jarvis SP, Barker PD ACS Nano. (2012) 6: 1332-1346 The polydispersity of αB-crystallin is rationalised by an interconverting polyhedral architecture Baldwin AJ, Lioe H, Hilton GR, Baker LA, Rubinstein JL, Kay LE, Benesch JLP Structure (2011) 19: 1855-63 Quaternary dynamics of αB-crystallin as a direct consequence of localised tertiary fluctuations in the C-terminus Baldwin AJ, Hilton GR, Lioe H, Bagnéris C, Benesch JLP, Kay LE J. Mol. Biol. (2011) 413: 310-20 αB-crystallin polydispersity is a consequence of unbiased quaternary dynamics Baldwin AJ, Lioe H, Robinson CV, Kay LE, Benesch JLP J. Mol. Biol. (2011) 413: 297-309 Metastability of native proteins towards amyloid formation Baldwin AJ, Knowles TPJ, Devlin GL, Shammas SL, Fitzpatrick AW, Waudby C, Mossuto MF, Meehan S, Gras SL, Christodoulou J, Anthony-Cahill SJ, Barker PD, Vendruscolo M, Dobson CM JACS (2011) 133: 14160-14163 Perturbation of the stability of amyloid fibrils through alteration of electrostatic interactions Shammas S, Knowles TPJ, Baldwin AJ, MacPhee CE, Welland ME, Dobson CM, Devlin GL Biophysical Journal (2011) 100: 2783-2791 The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated Benesch JLP, Aquilina JA, Baldwin AJ, Rekas A, Stengel F, Lindner R, Basha E, Devlin G, Horwitz J, Vierling E, Carver JA, Robinson CV Chem. Biol. (2010) 17: 1008-17