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Department of Biochemistry profile

Dr Sigurd Wilbanks

PositionSenior Lecturer
DepartmentDepartment of Biochemistry
QualificationsAB (Harv) PhD (Berk)
Research summaryStructure and function of Chaperones

Research

Our lab employs a variety of biophysical techniques to study protein conformational changes and enzyme mechanisms. We have a primary interest in the structure and function of molecular chaperones, the cell's main defense against stress-induced protein misfolding and aggregation. In recent years our research has expanded to include investigation of splicing mechanisms for protein inteins, cytochrome c, cysteine dioxygenase, Wilms' Tumor 1 protein, and Psb27, a component of photosystem II.

Publications

Fellner, M., Doughty, L. M., Jameson, G. N. L., & Wilbanks, S. M. (2014). A chromogenic assay of substrate depletion by thiol dioxygenases. Analytical Biochemistry, 459, 56-60. doi: 10.1016/j.ab.2014.05.008

Mabbitt, P. D., Wilbanks, S. M., & Eaton-Rye, J. J. (2014). Duplication and divergence of the Psb27 subunit of Photosystem II in the green algal lineage. New Zealand Journal of Botany, 52(1), 74-83. doi: 10.1080/0028825X.2013.859629

Tyndall, J. D. A., Lue, H., Rutledge, M. T., Bernhagen, J., Hampton, M. B., & Wilbanks, S. M. (2012). Macrophage migration inhibitory factor covalently complexed with phenethyl isothiocyanate. Acta Crystallographica Section F, 68(9), 999-1002. doi: 10.1107/s1744309112030552

Fagerlund, R. D., Ooi, P. L., & Wilbanks, S. M. (2012). Soluble expression and purification of tumor suppressor WT1 and its zinc finger domain. Protein Expression & Purification, 85(2), 165-172. doi: 10.1016/j.pep.2012.08.002

Tchesnokov, E. P., Wilbanks, S. M., & Jameson, G. N. L. (2012). A strongly bound high-spin iron(II) coordinates cysteine and homocysteine in cysteine dioxygenase. Biochemistry, 51(1), 527-564. doi: 10.1021/bi201597w

Journal - Research Article

Spencer, E. S., Dale, E. J., Gommans, A. L., Rutledge, M. T., Vo, C. T., Nakatani, Y., Gamble, A. B., Smith, R. A. J., Wilbanks, S. M., Hampton, M. B., & Tyndall, J. D. A. (2015). Multiple binding modes of isothiocyanates that inhibit macrophage migration inhibitory factor. European Journal of Medicinal Chemistry, 93, 501-510. doi: 10.1016/j.ejmech.2015.02.012

Josephs, T. M., Morison, I. M., Day, C. L., Wilbanks, S. M., & Ledgerwood, E. C. (2014). Enhancing the peroxidase activity of cytochrome c by mutation of residue 41: Implications for the peroxidase mechanism and cytochrome c release. Biochemical Journal, 458(2), 259-265. doi: 10.1042/BJ20131386

Mabbitt, P. D., Wilbanks, S. M., & Eaton-Rye, J. J. (2014). Duplication and divergence of the Psb27 subunit of Photosystem II in the green algal lineage. New Zealand Journal of Botany, 52(1), 74-83. doi: 10.1080/0028825X.2013.859629

Fellner, M., Doughty, L. M., Jameson, G. N. L., & Wilbanks, S. M. (2014). A chromogenic assay of substrate depletion by thiol dioxygenases. Analytical Biochemistry, 459, 56-60. doi: 10.1016/j.ab.2014.05.008

Josephs, T. M., Liptak, M. D., Hughes, G., Lo, A., Smith, R. M., Wilbanks, S. M., … Ledgerwood, E. C. (2013). Conformational change and human cytochrome c function: Mutation of residue 41 modulates caspase activation and destabilizes Met-80 coordination. Journal of Biological Inorganic Chemistry, 18, 289-297. doi: 10.1007/s00775-012-0973-1

Tchesnokov, E. P., Wilbanks, S. M., & Jameson, G. N. L. (2012). A strongly bound high-spin iron(II) coordinates cysteine and homocysteine in cysteine dioxygenase. Biochemistry, 51(1), 527-564. doi: 10.1021/bi201597w

Fagerlund, R. D., Ooi, P. L., & Wilbanks, S. M. (2012). Soluble expression and purification of tumor suppressor WT1 and its zinc finger domain. Protein Expression & Purification, 85(2), 165-172. doi: 10.1016/j.pep.2012.08.002

Tyndall, J. D. A., Lue, H., Rutledge, M. T., Bernhagen, J., Hampton, M. B., & Wilbanks, S. M. (2012). Macrophage migration inhibitory factor covalently complexed with phenethyl isothiocyanate. Acta Crystallographica Section F, 68(9), 999-1002. doi: 10.1107/s1744309112030552

Siakkou, E., Rutledge, M. T., Wilbanks, S. M., & Jameson, G. N. L. (2011). Correlating crosslink formation with enzymatic activity in cysteine dioxygenase. Biochimica et Biophysica Acta: Proteins & Proteomics, 1814, 2003-2009. doi: 10.1016/j.bbapap.2011.07.019

Liptak, M. D., Fagerlund, R. D., Ledgerwood, E. C., Wilbanks, S. M., & Bren, K. (2011). The proapoptotic G41S mutation to human cytochrome c alters the heme electronic structure and increases the electron self-exchange rate. Journal of the American Chemical Society, 133(5), 1153-1155. doi: 10.1021/ja106328k

Siakkou, E., Wilbanks, S. M., & Jameson, G. N. L. (2010). Simplified cysteine dioxygenase activity assay allows simultaneous quantitation of both substrate and product. Analytical Biochemistry, 405(1), 127-131. doi: 10.1016/j.ab.2010.06.013

Jackson, S. A., Fagerlund, R. D., Wilbanks, S. M., & Eaton-Rye, J. J. (2010). Crystal structure of PsbQ from Synechocystis sp. PCC 6803 at 1.8 Å: Implications for binding and function in cyanobacterial photosystem II. Biochemistry, 49(13), 2765-2767. doi: 10.1021/bi100217h

Kleffmann, T., Jongkees, S. A. K., Fairweather, G., Wilbanks, S. M., & Jameson, G. N. L. (2009). Mass-spectrometric characterization of two posttranslational modifications of cysteine dioxygenase. Journal of Biological Inorganic Chemistry, 14, 913-921. doi: 10.1007/s00775-009-0504-x

Mabbitt, P. D., Rautureau, G. J. P., Day, C. L., Wilbanks, S. M., Eaton-Rye, J. J., & Hinds, M. G. (2009). Solution structure of Psb27 from cyanobacterial photosystem II. Biochemistry, 48(37), 8771-8773. doi: 10.1021/bi901309c

Morison, I. M., Cramer Bordé, E. M., Cheesman, E. J., Cheong, P. L., Holyoake, A. J., Fichelson, S., Weeks, R. J., Lo, A., Davies, S. M. K., Wilbanks, S. M., Fagerlund, R. D., Ludgate, M. W., da Silva Tatley, F. M., Coker, M. S. A., Bockett, N. A., Hughes, G., Pippig, D. A., Smith, M. P., … Ledgerwood, E. C. (2008). A mutation of human cytochrome c enhances the intrinsic apoptotic pathway but causes only thrombocytopenia. Nature Genetics, 40(4), 387-389. doi: 10.1038/ng.103

Pearl, E. J., Bokor, A. A. M., Butler, M. I., Poulter, R. T. M., & Wilbanks, S. M. (2007). Preceding hydrophobic and β-branched amino acids attenuate splicing by the CnePRP8 intein. Biochimica et Biophysica Acta: General Subjects, 1774, 995-1001. doi: 10.1016/j.bbapap.2007.05.015

Pearl, E. J., Tyndall, J. D. A., Poulter, R. T. M., & Wilbanks, S. M. (2007). Sequence requirements for splicing by the Cne PRP8 intein. FEBS Letters, 581, 3000-3004.

Schlünzen, F., Wilson, D. N., Tian, P., Harms, J. M., McInnes, S. J., Hansen, H. A. S., … Wilbanks, S. M., & Fucini, P. (2005). The binding mode of the trigger factor on the ribosome: Implications for protein folding and SRP interaction. Structure, 13, 1-10.

MacKenzie, C. R., Wilbanks, S. M., & McGrath, K. M. (2004). Superimposed effect of kinetics and echinoderm glycoproteins on hierarchical growth of calcium carbonate. Journal of Materials Chemistry, 14, 1238-1244.

Sousa, M. C., Trame, C. B., Tsuruta, H., Wilbanks, S., Reddy, V. S., & McKay, D. (2000). Crystal and solution structures of an HSIUV protease - chaperone complex. Cell, 103, 633-643.

Wilbanks, S., & McKay, D. B. (1998). Structural replacement if active site monovalent cations by the e-amino group of Lysine in the ATPase fragment of bovine Hsc70. Biochemistry, 37, 7456-7462.

Ha, J.-H., Hellman, U., Johnson, E. R., Li, L., McKay, B. D., Sousa, M. C., … Wilbanks, S. (1997). Destablization of peptide binding by an E543K mutation in the seventy kilodalton bovine heat shock cognate protein, a molecular chaperone. Journal of Biological Chemistry, 272, 27796-27803.

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