Dr. Christina Redfield

Biography

Christina Redfield is a renowned researcher in the field of Biochemistry, focusing on protein structure, function, and folding dynamics using nuclear magnetic resonance (NMR) spectroscopy. Her work provides atomic-level insights into biological macromolecules, including proteins and nucleic acids, in a native-like environment. Redfield's group employs NMR in diverse ways to determine protein structures in solution, study backbone dynamics over a range of timescales, characterize partially-folded molten globule states, and investigate protein-protein interactions. With access to NMR spectrometers operating at 1H frequencies between 500 and 950 MHz located in the Department of Biochemistry, she conducts highly collaborative research with various groups within the Medical Sciences Division. Recent projects have focused on understanding the specificity and reactivity of the bacterial transmembrane oxidoreductase DsbD, studying the structure and dynamics of EGF-like domains in proteins such as fibrillin-1 and LTBP Notch-1, and using NMR to investigate the structure and dynamics of proteins involved in bacterial chemotaxis. Additionally, she has characterized determinants affecting the structure and stability of molten globule states in proteins such as α-lactalbumin.

Research Interests