Guy Dodson's major researches have been concerned with the Xray analysis of a variety of crystalline proteins many now being carried out with increasing speed and accuracy through the use of synchrotron radiation. His most considerable work, on insulin, extends from his part in the first solution of the 2 zinc insulin crystal structure to the refeinement of the atomic parameters of both protein and water moledules at 1.5A resolution. He has recently explored remarkable conformational variations of the insulin molecule under different conditions, which give rise to three different hexamers, dimers at different pH and a monomeric despentapeptide insulin. He is at present investigating structure activity relations of genetically engineered varieties of insulin. Other systems he has studied include a series of bacterial ribonucleases and the T state of haemoglobin as seen in the partially liganded T alpha oxy beta deoxy, T alpha met beta met and T alpha deoxy beta deoxy human haemoglobins, crystallised from polyethyleneglycol. It is characteristic of him that he has created a laboratory to which protein crystals are brought from all over the world and their structures solved.
^Davies, G. J.; Dodson, G. G.; Hubbard, R. E.; Tolley, S. P.; Dauter, Z.; Wilson, K. S.; Hjort, C.; Mikkelsen, J. M. L.; Rasmussen, G.; Schülein, M. (1993). "Structure and function of endoglucanase V". Nature. 365 (6444): 362–4. Bibcode:1993Natur.365..362D. doi:10.1038/365362a0. PMID8377830.
^Brzozowski, A. M.; Derewenda, U.; Derewenda, Z. S.; Dodson, G. G.; Lawson, D. M.; Turkenburg, J. P.; Bjorkling, F.; Huge-Jensen, B.; Patkar, S. A.; Thim, L. (1991). "A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex". Nature. 351 (6326): 491. Bibcode:1991Natur.351..491B. doi:10.1038/351491a0. PMID2046751.
^Brady, L.; Brzozowski, A. M.; Derewenda, Z. S.; Dodson, E.; Dodson, G.; Tolley, S.; Turkenburg, J. P.; Christiansen, L.; Huge-Jensen, B.; Norskov, L.; Thim, L.; Menge, U. (1990). "A serine protease triad forms the catalytic centre of a triacylglycerol lipase". Nature. 343 (6260): 767–70. Bibcode:1990Natur.343..767B. doi:10.1038/343767a0. PMID2304552.
^Perutz, M. F.; Wilkinson, A. J.; Paoli, M.; Dodson, G. G. (1998). "The Stereochemical Mechanism of the Cooperative Effects in Hemoglobin Revisited". Annual Review of Biophysics and Biomolecular Structure. 27: 1. doi:10.1146/annurev.biophys.27.1.1.