Skip to main content
Skip to main menu Skip to spotlight region Skip to secondary region Skip to UGA region Skip to Tertiary region Skip to Quaternary region Skip to unit footer

Slideshow

Barb

Our laboratory determined that N-glycosylation of a circulating immunoglobulin was required for receptor binding because long-range contacts within the antibody molecule stabilize key residues to form an interface with the receptor. We believe, based on these results and the high frequency of N-glycan addition to secreted proteins, that comparable mechanisms are likely found throughout the body but remain undescribed due to technological limitations. We developed a multi-technique strategy utilizing solution nuclear magnetic resonance spectroscopy, mass spectrometry, recombinant protein expression and stable isotope labeling as well as isolation and high-resolution characterization of proteins from primary human tissue to surmount this obstacle. We are currently applying and expanding this platform to identify new N-glycans that modulate protein function by focusing on the immune system where we expect to find countless more examples. A high-resolution definition of novel cell-mediated variables that affect function will provide insight into cell function and will form the foundation for future therapies to promote health and alleviate disease.

Support us

We appreciate your financial support. Your gift is important to us and helps support critical opportunities for students and faculty alike, including lectures, travel support, and any number of educational events that augment the classroom experience. Click here to learn more about giving.

Every dollar given has a direct impact upon our students and faculty.