Judith Herzfeld (born 12 January 1948) is Professor of Biophysical Chemistry at Brandeis University. Known for her work in statistical thermodynamics, solid state NMR and chemical education, she is a fellow of the American Physical Society, the American Association for the Advancement of Science, and the Massachusetts Academy of Sciences. She is the author or coauthor of more than 180 scientific papers and a book.
Although trained as a theoretician, Herzfeld's interest in biophysics led her to also establish an experimental program.
For the first two decades, her theoretical program focused on the spontaneous spatial ordering of self-assembled protein filaments in the crowded interiors of cells and its implications for the morphology and rheology of cells in health and in disease (e.g., sickle-cell disease). More recently, her theoretical program has focused on developing an explicit valence electron force field (LEWIS) for efficient modeling of reactions in complex solvents, so that detailed computer simulations can provide insights into solvent influences on reaction mechanisms, rates and selectivity.
Her experimental program applies solid state NMR spectroscopy to problems that are intractable by other structural methods. A long-term study has focused on the mechanism by which the membrane protein bacteriorhodopsin executes ion transfers that convert light energy to electrochemical form. A more recent study on the floatation organelles of aquatic micro-organisms has revealed that an amyloid pattern of protein assembly underlies their strength and interfacial stability. Other studies have elucidated the structures of amorphous polymers that form under prebiotic conditions. In the course of solving some of the practical problems involved in this work, she has also developed some methods that have been adopted by other spectroscopists. This includes spinning sideband analysis to extract local anisotropy information, and spectroscopy by the integration of frequency and time domain information (SIFT) to carryout rapid, model-free processing of non-uniformly sampled spin evolution.