Elizabeth Marie Nolan (born 1978) is an American chemist and associate professor at Massachusetts Institute of Technology.

Nolan was born in Niskayuna, New York.^[1] She studied at Smith College, where she majored in chemistry and graduated magna cum laude in 2000.^[1][2] During her undergraduate studies she minored in music and worked with Robert Linck on computational chemistry.^[3] She studied the stereoelectronic effects in substituted alkanes.^[4] Nolan was a member of Phi Beta Kappa.^[1] She was awarded a Fulbright Program Scholarship and moved to France to study siderophore-iron complexes.^[2] Nolan moved to Massachusetts Institute of Technology for her graduate studies, where she was supervised by Stephen J. Lippard.^[1] She developed small molecule fluorescent sensors to monitor for zinc in neurobiology and mercury in aqueous solutions.^[1][5] Together they filed a patent for Fluorescein-based metal sensors.^[6] Nolan was a postdoctoral scientist at the Harvard Medical School, working with Christopher T. Walsh on the biosynthetic assembly of microcin E492m.^[7] Microcin E492m is an antibiotic peptide that can target Gram-negative bacteria which express siderophore transporters.^[1][7][8] She was awarded a $2.5 million National Institutes of Health grant in 2010 to study antibacterial peptides and zinc in innate immunity.^[9] In 2011 she contributed to the book Letters to a Young Chemist.^[4][10]

Nolan was appointed as an assistant professor at the department of chemistry at the Massachusetts Institute of Technology in 2014.^[1] She explores the coordination chemistry of metal ions in biological systems; in particular how proteins destroy microbes by denying them metal nutrients.^[3][11][12] She looks at the peptides and metalloproteins that are involved in mammalian immune response. Her current focus is on calprotectins and how they bind metals.^[13][14] She used magnetic circular dichroism to study the binding of iron to human calprotectin.^[15] Her group look to understand how Neuronal cells process and removes SOD1 point mutants.^[16]

Nolan looks to design drugs to fight bacterial infections.^[11] They study how immunity peptides that are encoded by the gene clusters that biosynthesize antibiotics which use metal ion transporters protect the organisms that produce them.^[16] She proposes that hijacking the siderophore uptake pathways could allow new prevention and treatment against diseases.^{[citation needed]} She worked with Manuela Raffatellu at University of California, Irvine to develop a new immunisation strategy against salmonella.^[17] They target siderophores, a molecule that salmonella secretes to scavenge iron. Immunisation against siderophores led to the production of antibodies that reduced the growth of salmonella and other bacteria.^[18] She is on the editorial board of Cell Chemical Biology.^[19]