C. Macdonald

发表

The structural and energetic basis for high selectivity in a high-affinity protein-protein interaction

D. Baker, S. Fleishman, Nicola A. G. Meenan, 2010, Proceedings of the National Academy of Sciences.

The Two-State Prehensile Tail of the Antibacterial Toxin Colicin N

C. Macdonald, G. Moore, J. G. Grossmann, 2017, Biophysical journal.

Synthesis and characterization of some octaalkyl substituted lead phthalocyanines and unexpected variations in lead lability arising from the position of substituents and their chain length

C. Macdonald, S. Coles, G. Tizzard, 2013 .

Identification and characterisation of a G-quadruplex forming sequence in the promoter region of nuclear factor (erythroid-derived 2)-like 2 (Nrf2).

Zoë A. E. Waller, C. Macdonald, M. O'Connell, 2014, Biochemical and biophysical research communications.

Structural Evidence That Colicin A Protein Binds to a Novel Binding Site of TolA Protein in Escherichia coli Periplasm

Chan Li, C. Macdonald, G. Moore, 2012, The Journal of Biological Chemistry.

Spin Saturation Transfer Difference NMR (SSTD NMR): A New Tool to Obtain Kinetic Parameters of Chemical Exchange Processes

J. Angulo, C. Macdonald, M. Muñoz, 2016, Journal of visualized experiments : JoVE.

Transformation of a methyleneamide ligand at molybdenum: electrochemical oxidation to a cyanide, reactions with elemental oxygen, sulphur or selenium and X-ray crystal structures of trans-[Mo(CN)Cl(dppe)2]·MeOH and trans-[Mo(NCS)Cl(dppe)2]; electroreduction of the cyanide to an aminocarbyne, trans-[

C. Macdonald, A. Hills, C. Pickett, 1991 .

Electrochemistry of ligands multiply bonded to molybdenum and tungsten

C. Macdonald, D. Lowe, C. Pickett, 1989 .

Metal hydrides as intermediates in the reactions of coordinated unsaturated hydrocarbons: formation of propyne by protonation of trans- [WH(η3-C5H5) (Ph2PCH2CH2PPh2)2]

C. Macdonald, R. Henderson, D. Hughes, 1997 .

Fixing the Conformation of Calix[4]arenes: When Are Three Carbons Not Enough?

C. Macdonald, S. E. Matthews, S. Vidal, 2018, Chemistry.

Electrosynthesis of amino acids from a molybdenum nitride via nitrogen–carbon and carbon–carbon bond formation reactions involving imides and nitrogen ylides: X-ray structure of trans-[MoCl(NCHCO2Me)(Ph2PCH2CH2PPh2)2]·CH2Cl2

C. Macdonald, C. Pickett, D. Hughes, 1992 .

The chemistry of niobium and tantalum dithiocarbamato-complexes. Part 1. Synthesis, structure, and protonation of dinitrogen-bridged complexes

D. Walton, C. Macdonald, A. Hills, 1990 .

NMR spectroscopic evidence for the self-association of some asymmetrically substituted phthalocyanines in solution

Denise A. Mayes, C. Macdonald, I. Chambrier, 2003 .

Redox-dependent control of i-Motif DNA structure using copper cations

Zoë A. E. Waller, C. Macdonald, L. Fábián, 2018, Nucleic acids research.

NMR Spectroscopy as a Probe for DMSP and Glycine Betaine in Phytoplankton Cells

C. Macdonald, G. Moore, G. Malin, 1996 .

Clusters in an intrinsically disordered protein create a protein-binding site: the TolB-binding region of colicin E9.

C. Macdonald, G. Moore, C. Kleanthous, 2005, Biochemistry.

Characterisation of a mobile protein-binding epitope in the translocation domain of colicin E9

C. Macdonald, G. Moore, C. Kleanthous, 2004, Journal of biomolecular NMR.

Synthesis of the branched-chain sugar aceric acid: a unique component of the pectic polysaccharide rhamnogalacturonan-II.

C. Macdonald, R. Field, S. Nepogodiev, 2005, The Journal of organic chemistry.

Heightened Dynamics of the Oxidized Y48H Variant of Human Cytochrome c Increases Its Peroxidatic Activity.

C. Macdonald, G. Moore, Michael T. Wilson, 2017, Biochemistry.

Helix N-Cap Residues Drive the Acid Unfolding That Is Essential in the Action of the Toxin Colicin A

C. Macdonald, G. Moore, Christopher L. Johnson, 2019, Biochemistry.

Concerted Folding and Binding of a Flexible Colicin Domain to Its Periplasmic Receptor TolA*

Gregor Anderluh, C. Macdonald, R. Boetzel, 2003, Journal of Biological Chemistry.

Backbone resonance assignments of ferric human cytochrome c and the pro-apoptotic G41S mutant in the ferric and ferrous states

C. Macdonald, G. Moore, J. Worrall, 2015, Biomolecular NMR Assignments.

Backbone resonance assignments of ferric human cytochrome c and the pro-apoptotic G41S mutant in the ferric and ferrous states

C. Macdonald, G. Moore, J. Worrall, 2015, Biomolecular NMR assignments.

Increased dynamics in the 40–57 Ω-loop of the G41S variant of human cytochrome c promote its pro-apoptotic conformation

C. Macdonald, G. Moore, Michael T. Wilson, 2016, Scientific Reports.

Intrinsically disordered proteins: lessons from colicins.

C. Macdonald, G. Moore, Oliver Hecht, 2012, Biochemical Society transactions.

Structural dynamics of the membrane translocation domain of colicin E9 and its interaction with TolB.

C. Macdonald, R. Boetzel, G. Moore, 2002, Journal of molecular biology.

Saturation transfer difference NMR on the integral trimeric membrane transport protein GltPh determines cooperative substrate binding

H. Sitte, J. Angulo, C. Macdonald, 2020, Scientific Reports.

Reversible DNA i-motif to hairpin switching induced by copper(ii) cations

H. Day, Zoë A. E. Waller, C. Macdonald, 2015, Chemical communications.

Near-complete backbone resonance assignments of acid-denatured human cytochrome c in dimethylsulfoxide: a prelude to studying interactions with phospholipids

C. Macdonald, G. Moore, J. Worrall, 2017, Biomolecular NMR assignments.

Biophysical Features of Bacillithiol, the Glutathione Surrogate of Bacillus subtilis and other Firmicutes

C. Macdonald, Sunil V Sharma, C. Hamilton, 2013, Chembiochem : a European journal of chemical biology.

Carbon‐13 and related NMR chemical shifts in alkylammonium and alkylphosphonium salts

C. Macdonald, David J Evans, G. Leigh, 1990 .

Interactions of TolB with the Translocation Domain of Colicin E9 Require an Extended TolB Box

C. Macdonald, G. Moore, R. James, 2005, Journal of bacteriology.

NMR detection of slow conformational dynamics in an endonuclease toxin

A. Pommer, C. Macdonald, R. Boetzel, 1998, Journal of biomolecular NMR.