研究领域

Theoretical/Biological

Our research focuses on different aspects of how proteins fold and how large protein complexes assemble. Projects cover diverse areas including biophysics, molecular biology (including protein engineering) and chemical biology. Current projects include: How does a knotted protein fold? Recently, a remarkable new class of proteins have been discovered which have deep topological knots formed by the polypeptide backbone. These structures represent a new challenge for the protein folding community - not only has the protein to fold but in doing so it must also knot. We are studying the folding pathways of several knotted proteins, including YibK shown on the right, using a combination of experimental and computational techniques. How do molecular chaperones work to assembly large molecular complexes? Heat shock protein 90 (Hsp90) is a highly abundant and important protein in our cells which is the target of a new class of anti-tumour agents. It plays a key role in the assembly of a number of cellular complexes which are critical in cellular signal transduction pathways. We are combining a large number of biophysical techniques to understand the mode of action of Hsp90. Single molecule studies on the folding of a large β-barrel protein. The green fluorescent protein (GFP) first isolated from jellyfish is a protein with unique spectroscopic properties. A cyclisation and oxidation of the polypeptide backbone results in the formation of a chromophore which is highly fluorescent. In collaboration with the Klenerman group are using these special features of GFP to study the folding of this protein at a single molecule level.

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Mechanistic Insights into the Folding of Knotted Proteins In Vitro and In Vivo NC Lim, SE Jackson – Journal of molecular biology (2015) 427, 248 (DOI: 10.1016/j.jmb.2014.09.007) Bayesian inference of accurate population sizes and FRET efficiencies from single diffusing biomolecules. RR Murphy, G Danezis, MH Horrocks, SE Jackson, D Klenerman – Anal Chem (2014) 86, 8603 (DOI: 10.1021/ac501188r) Mechanistic Insights Into The Folding Of The Trefoil-Knotted Proteins NC Lim, SE Jackson – PROTEIN SCIENCE (2014) 23, 239 Tau-Hsp70 Interaction at the Single-Molecule Level F Kundel, M Kjaergaard, SL Shammas, SE Jackson, D Klenerman – BIOPHYSICAL JOURNAL (2014) 106, 59A Hsp90 Inhibits alpha-Synuclein Aggregation by Interacting with Soluble Oligomers S Daturpalli, CA Waudby, S Meehan, SE Jackson – Journal of molecular biology (2013) 425, 4614 (DOI: 10.1016/j.jmb.2013.08.006) Accurate Intramolecular Distances by Single Molecule Confocal Spectroscopy: A Monte Carlo Markov Chain Analysis of Fluorescence Data from Freely Diffusing Biomolecules RR Murphy, G Danezis, SE Jackson, D Klenerman – BIOPHYSICAL JOURNAL (2013) 104, 174A Backbone NMR assignments of a topologically knotted protein in urea-denatured state S-JM Hsieh, AL Mallam, SE Jackson, S-TD Hsu – Biomolecular NMR Assignments (2013) 1 (DOI: 10.1007/s12104-013-9510-6) Backbone NMR assignments of a topologically knotted protein in urea-denatured state S-JM Hsieh, AL Mallam, SE Jackson, S-TD Hsu – Biomolecular NMR Assignments (2013) 1 (DOI: 10.1007/s12104-013-9501-7) Erratum to: Backbone 1H, 13C and 15N assignments of YibK and a variant containing a unique cysteine residue at C-terminus in 8 M urea-denatured states S-JM Hsieh, AL Mallam, SE Jackson, S-TD Hsu – Biomolecular NMR Assignments (2013) 1 (DOI: 10.1007/s12104-013-9519-x) Hsp90 inhibits α-synuclein aggregation by interacting with soluble oligomers S Daturpalli, CA Waudby, S Meehan, SE Jackson – Journal of Molecular Biology (2013) 425, 4614 (DOI: 10.1016/j.jmb.2013.08.006) Molecular Chaperones Preface SE Jackson – MOLECULAR CHAPERONES (2013) 328, V Distinct mechanisms of calmodulin binding and regulation of adenylyl cyclases 1 and 8 N Masada, S Schaks, SE Jackson, A Sinz, DM Cooper – Biochemistry (2012) 51, 7917 (DOI: 10.1021/bi300646y) Hsp90: Structure and function SE Jackson – Top Curr Chem (2013) 328, 155 (DOI: 10.1007/128_2012_356) Ubiquitin chain conformation regulates recognition and activity of interacting proteins Y Ye, G Blaser, MH Horrocks, MJ Ruedas-Rama, S Ibrahim, AA Zhukov, A Orte, D Klenerman, SE Jackson, D Komander – Nature (2012) 492, 266 (DOI: 10.1038/nature11722) Knot formation in newly translated proteins is spontaneous and accelerated by chaperonins AL Mallam, SE Jackson – Nature Chemical Biology (2011) 8, 147 (DOI: 10.1038/nchembio.742) Heterogeneity and dynamics in the assembly of the Heat Shock Protein 90 chaperone complexes IO Ebong, N Morgner, M Zhou, MA Saraiva, S Daturpalli, SE Jackson, CV Robinson – Proceedings of the National Academy of Sciences of the United States of America (2011) 108, 17939 (DOI: 10.1073/pnas.1106261108) The effect of Parkinson's-disease-associated mutations on the deubiquitinating enzyme UCH-L1. FI Andersson, EF Werrell, L McMorran, WJ Crone, C Das, ST Hsu, SE Jackson – Journal of molecular biology (2011) 407, 261 (DOI: 10.1016/j.jmb.2010.12.029) A high-throughput fluorescence chemical denaturation assay as a general screen for protein-ligand binding K Mahendrarajah, PA Dalby, B Wilkinson, SE Jackson, ER Main – Analytical Biochemistry (2011) 411, 155 (DOI: 10.1016/j.ab.2010.12.001) Experimental detection of knotted conformations in denatured proteins. AL Mallam, JM Rogers, SE Jackson – Proceedings of the National Academy of Sciences of the United States of America (2010) 107, 8189 (DOI: 10.1073/pnas.0912161107) Backbone assignments of the 26 kDa neuron-specific ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1). FI Andersson, SE Jackson, ST Hsu – Biomolecular NMR Assignments (2010) 4, 41 (DOI: 10.1007/s12104-009-9203-3)