Distinguished Professor

Prof. Ted Baker


Research Synopsis
  • Protein structure and function
  • The molecular basis of biological processes


Photo of Prof. Ted Baker
Telephone:  09-373-7599 ext 84415
Office:  Room 470, Thomas Building
E-mail:ted.baker@auckland.ac.nz


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Research


Research in our group is concerned with determining the molecular basis of biological processes. We focus on the structure and function of proteins, using X-ray crystallography to determine their 3D structures, and various approaches to relate structure to function (kinetics, binding studies, recombinant DNA methods, as appropriate). Some projects are directed towards the design of new therapeutic drugs. Research is likely to involve Students will also have the opportunity (in some projects) to learn techniques of DNA manipulation and protein engineering.


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Projects


Current projects include the following:




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More Publications   

Recent Publications


Arcus VL, Langley R, Proft T, Fraser JD and Baker EN   The three-dimensional structure of a superantigen-like protein, SET3, from a pathogenicity island of the Staphylococcus aureus genome.   Journal of Biological Chemistry. 277(35):32274-32281, 2002 Aug 30.   View Abstract

Baker EN and Wittinghofer A   Proteins - from little acorns mighty oak trees grow - Editorial overview.   Current Opinion in Structural Biology. 12(6):743-745, 2002 Dec.  

Baker EN, Baker HM and Kidd RD   Lactoferrin and transferrin: Functional variations on a common structural framework.   Biochemistry & Cell Biology-Biochimie & Biologie Cellulaire|Biochemistry and Cell Biology-Biochimie et Biologie Cellulaire. 80(1):27-34, 2002 Feb.   View Abstract

Brittain T, Kidd RD and Baker EN   Electron transfer between cytochrome b(5) and some oxidised haemoglobins: the role of ionic strength.   Journal of Inorganic Biochemistry. 88(3-4):328-334, 2002 Feb.   View Abstract

Jameson GB, Anderson BF, Breyer WA, Day CL, Tweedie JW and Baker EN   Structure of a domain-opened mutant (R121D) of the human lactoferrin N-lobe refined from a merohedrally twinned crystal form.   Acta Crystallographica Section D-Biological Crystallography. 58(Part 6 Special Issue 2):955-962, 2002 Jun.   View Abstract

Kidd RD, Baker EN and Brittain T   A modeling study of the interaction and electron transfer between cytochrome b(5) and some oxidized haemoglobins.   Journal of Biological Inorganic Chemistry. 7(1-2):23-30, 2002 Jan.   View Abstract

Peterson NA, Arcus VL, Anderson BF, Tweedie JW, Jameson GB and Baker EN   Dilysine trigger in transferrins probed by mutagenesis of lactoferrin: Crystal structures of the R210G, R210E, and R210L mutants of human lactoferrin.   Biochemistry. 41(48):14167-14175, 2002 Dec 3.   View Abstract

Baker HM, Mason AB, He QY, MacGillivray RTA and Baker EN   Ligand variation in the transferrin family: The crystal structure of the H249Q mutant of the human transferrin N-lobe as a model for iron binding in insect transferrins.   Biochemistry. 40(39):11670-11675, 2001 Oct 2.   View Abstract

Banfield MJ, Lott JS, Arcus VL, McCarthy AA and Baker EN   Structure of HisF, a histidine biosynthetic protein from Pyrobaculum aerophilum.   Acta Crystallographica Section D-Biological Crystallography. 57(Part 11):1518-1525, 2001 Nov.   View Abstract

Banfield MJ, Salvucci ME, Baker EN and Smith CA   Crystal structure of the NADP(H)-dependent ketose reductase from Bemisia argentifolii at 2.3 angstrom resolution.   Journal of Molecular Biology. 306(2):239-250, 2001 Feb 16.   View Abstract

Edwards RA, Whittaker MM, Whittaker JW, Baker EN and Jameson GB   Outer sphere mutations perturb metal reactivity in manganese superoxide dismutase.   Biochemistry. 40(1):15-27, 2001 Jan 9.   View Abstract

Edwards RA, Whittaker MM, Whittaker JW, Baker EN and Jameson GB   Removing a hydrogen bond in the dimer interface of Escherichia coli manganese superoxide dismutase alters structure and reactivity.   Biochemistry. 40(15):4622-4632, 2001 Apr 17.   View Abstract

Haebel PW, Arcus VL, Baker EN and Metcalf P   LISA: an intranet-based flexible database for protein crystallography project management.   Acta Crystallographica Section D-Biological Crystallography. 57(Part 9):1341-1343, 2001 Sep.   View Abstract

Harrak H, Azelmat S, Baker EN and Tabaeizadeh Z   Isolation and characterization of a gene encoding a drought-induced cysteine protease in tomato (Lycopersicon esculentum).   Genome. 44(3):368-374, 2001 Jun.   View Abstract

Kidd RD, Baker HM, Mathews AJ, Brittain T and Baker EN   Oligomerization and ligand binding in a homotetrameric hemoglobin: Two high-resolution crystal structures of hemoglobin Bart's (gamma(4)), a marker for alpha-thalassemia.   Protein Science. 10(9):1739-1749, 2001 Sep.   View Abstract

Kidd RD, Mathews A, Baker HM, Brittain T and Baker EN   Subunit dissociation and reassociation leads to preferential crystallization of haemoglobin Bart's (gamma 4) from solutions of human embryonic haemoglobin Portland (zeta(2)gamma(2)) at low pH.   Acta Crystallographica Section D-Biological Crystallography. 57(Part 6):921-924, 2001 Jun.   View Abstract

Kidd RD, Russell JE, Watmough NJ, Baker EN and Brittain T   The role of beta chains in the control of the hemoglobin oxygen binding function: Chimeric human/mouse proteins, structure, and function.   Biochemistry. 40(51):15669-15675, 2001 Dec 25.   View Abstract

McCarthy AA, Baker HM, Shewry SC, Kagawa TF, Saafi E, Patchett ML and Baker EN   Expression, crystallization and preliminary characterization of methylmalonyl coenzyme A epimerase from Propionibacterium shermanii.   Acta Crystallographica Section D-Biological Crystallography. 57(Part 5):706-708, 2001 May.   View Abstract

McCarthy AA, Baker HM, Shewry SC, Patchett ML and Baker EN   Crystal structure of methylmalonyl-coenzyme A epimerase from P-shermanii: a novel enzymatic function on an ancient metal binding scaffold.   Structure. 9(7):637-646, 2001 Jul 3.   View Abstract

Moore SA, Kingston RL, Loomes KM, Hernell O, Blackberg L, Baker HM and Baker EN   The structure of truncated recombinant human bile salt-stimulated lipase reveals bile salt-independent conformational flexibility at the active-site loop and provides insights into heparin binding.   Journal of Molecular Biology. 312(3):511-523, 2001 Sep 21.   View Abstract



top Last updated 23 Mar 2007