Department of Chemistry

portrait of Professor Christopher Abell FMedSci

Professor Christopher Abell FMedSci

Christ's College

Groups: Abell group website

Telephone: 01223 336405

E-mail: ca26@cam.ac.uk

One of the biggest challenges in biological chemistry is the design of small molecules that interact selectively with macromolecules. We are pioneering the development of the use of fragments to address this challenge. This approach involves close synergistic interaction between synthetic organic chemistry, biophysics and structural biology. We are using fragment-based methods to identify inhibitors of enzymes from Mycobacterium tuberculosis, and to develop small molecules that modulate protein-protein interactions. We are also keen to explore new applications for fragments e.g. to identify molecules that modulate the activity of riboswitches, and to assign function to orphan proteins.

Our second major area of research is to develop the use of microdroplets in microfluidics as a novel experimental platform for biological chemistry. This research is highly interdisciplinary and involves biological chemistry, microfluidics, nanofabrication, laser spectroscopy and mass spectrometry. We are particularly interested in looking at cells in droplets, e.g. bacteria to study quorum sensing, algae for bio-fuel development.

 

Publications

Uroporphyrinogen III synthase: Studies on its mechanism of action, molecular biology and biochemistry
N CROCKETT, PR ALEFOUNDER, AR BATTERSBY, C ABELL - Tetrahedron (1991) 47, 6003
(DOI: 10.1016/S0040-4020(01)86492-9)
An amino acid sequence motif observed amongst enzymes of the shikimate pathway [1]
TDH BUGG, PR ALEFOUNDER, C ABELL - Biochemical Journal (1991) 276, 841
Studies on the mechanism of hydroxymethylbilane synthase concerning the role of arginine residues in substrate binding.
M LANDER, AR PITT, PR ALEFOUNDER, D BARDY, C ABELL, AR BATTERSBY - Biochemical Journal (1991) 275 ( Pt 2), 447
THE SYNTHESIS OF (6R)-[6-H-2]-5-ENOLPYRUVYLSHIKIMATE-3-PHOSPHATE AND (6S)-[6-H-2]-5-ENOLPYRUVYLSHIKIMATE-3-PHOSPHATE
S BALASUBRAMANIAN, C ABELL - TETRAHEDRON LETT (1991) 32, 963
(DOI: 10.1016/S0040-4039(00)92131-2)
Terpenoid biosynthesis and the stereochemistry of enzyme-catalysed allylic addition-elimination reactions
DE Cane, C Abell, PHM Harrison, BR Hubbard, CT Kane, R Lattman, JS Oliver, SW Weiner - (1991) 332, 123
Observation of an isotope effect in the chorismate synthase reaction
S BALASUBRAMANIAN, C ABELL, JR COGGINS - Journal of the American Chemical Society (1990) 112, 8581
(DOI: 10.1021/ja00179a052)
INVESTIGATION OF PUTATIVE ACTIVE-SITE LYSINE RESIDUES IN HYDROXYMETHYLBILANE SYNTHASE - PREPARATION AND CHARACTERIZATION OF MUTANTS IN WHICH (A) LYS-55, (B) LYS-59 AND (C) BOTH LYS-55 AND LYS-59 HAVE BEEN REPLACED BY GLUTAMINE
A HADENER, PR ALEFOUNDER, GJ HART, C ABELL, AR BATTERSBY - Biochemical Journal (1990) 271, 487
Biosynthesis of pentalenene and pentalenolactone
DE Cane, JS Oliver, PHM Harrison, C Abell, BR Hubbard, CT Kane, R Lattman - Journal of the American Chemical Society (1990) 112, 4513
(DOI: 10.1021/ja00167a059)
Isolation and characterisation of a cDNA clone for a chlorophyll synthesis enzyme from Euglena gracilis. The chloroplast enzyme hydroxymethylbilane synthase (porphobilinogen deaminase) is synthesised with a very long transit peptide in Euglena.
AL SHARIF, AG SMITH, C ABELL - Eur J Biochem (1989) 184, 353
(DOI: 10.1111/j.1432-1033.1989.tb15026.x)
Evidence that pyridoxal phosphate modification of lysine residues (Lys-55 and Lys-59) causes inactivation of hydroxymethylbilane synthase (porphobilinogen deaminase)
AD Miller, LC Packman, GJ Hart, PR Alefounder, C Abell, AR Battersby - Biochemical Journal (1989) 262, 119

 


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