Max Legg

Max Legg is a science advisor in in Goodwin’s Business Law department and a member of its Life Sciences Intellectual Property practice group. Dr. Legg joined Goodwin in 2022. Dr. Legg assists clients with a number of aspects related to intellectual property protections for life sciences innovations, including patent preparation, patent prosecution, freedom-to-operate analysis, and IP due diligence. Dr. Legg earned his PhD from the University of Victoria. His doctoral research focused on the structural characterization of S-layer proteins.

Prior to joining Goodwin, Max earned his PhD in Biochemistry at the University of Victoria (Victoria, British Columbia, Canada), where his research focused on the structure-function characterization of the bacterial surface proteins, monoclonal antibodies, as well as the human ABO(H) blood group-synthesizing enzymes. His work on these topics resulted in multiple publications in high-impact, peer-reviewed scientific journals. Max has been the recipient of multiple awards, including international- and national-level scholarships, recognizing his research and academic leadership.

• Canada Natural Sciences and Engineering Research Council (NSERC) Canada Graduate Doctoral Award, 2019–2022
• NSERC Canada Graduate Master's Scholarship, 2017

• Author, “Advancing understanding of secondary cell wall polymer binding and synthesis in S-layers of Gram-Positive bacteria,” Doctoral dissertation, University of Victoria in Victoria, B.C., Canada; uri: hdl.handle.net/1828/13865, 2022
• First-Author, “Monoclonal antibody 7H2.2 binds the C-terminus of the cancer-oocyte antigen SAS1B through the hydrophilic face of a conserved amphipathic helix corresponding to one of only two regions predicted to be ordered,” Acta Crystallographica Section D; doi: 10.1107/S2059798322003011, 2022
• Co-Author, “Antigen binding by conformational selection in near-germline antibodies,” Journal of Biological Chemistry; doi: 10.1016/j.jbc.2022.101901, 2022 
• First-Author, “The S-layer homology domains of Paenibacillus alvei surface protein SpaA bind to cell wall polysaccharide through the terminal monosaccharide residue,” Journal of Biological Chemistry; doi: 10.1016/j.jbc.2022.101745, 2022
• Co-Author, “Temperature-sensitive recombinant subtilisin protease variants that efficiently degrade molecular biology enzymes,” FEMS Microbiology Letters; doi: 10.1093/femsle/fnaa162, 2020
• Co-Author, “Conserved residues Arg188 and Asp302 are critical for active site organization and catalysis in human ABO(H) blood group A and B glycosyltransferases,” Glycobiology; doi: 10.1093/glycob/cwy051, 2018
• Co-First-Author, “High-resolution crystal structures and STD NMR mapping of human ABO(H) blood group glycosyltransferases in complex with trisaccharide reaction products suggest a molecular basis for product release,” Glycobiology; doi: 10.1093/glycob/cwx053, 2017