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D. Travis Gallagher (Fed)

Research Chemist

Travis Gallagher studied Electrical Engineering and Computer Science at MIT, and then Biochemistry at the University of Texas (Ph.D. 1990). After a National Research Council postdoctoral fellowship in protein crystallography with Gary Gilliland, he joined NIST's Biotechnology Division, leading to his present position at NIST/IBBR. 

Travis's interests in crystal growth, structure determination and the functional properties of proteins helped prepare him to grapple with key measurement and modeling challenges in the Biomolecular Measurement Dvision. His work advances the NIST mission by providing measurements and structural data on biomolecular models that are widely used in the commercial development of new protein medicines like antibodies and T cell receptors. 

For example, our 20659-atom 3D coordinate model of the NISTmAb monoclonal antibody standard reference material, based on extensive collaboration as well as Travis's crystallography and modeling, serves as a resource for the structural engineering that underlies the development of new immunotherapies. Another example is structural measurements of T cell receptors, which, like antibodies, are both vital to human health and in development for innovative medical applications. Beyond those specific projects, he collaborates widely with both UMD and NIST researchers on problems involving biomolecular measurements and models.

Selected Publications

Publications

Effects of Glycans and Hinge on Dynamics in the IgG1 Fc

Author(s)
Christina Bergonzo, J. Todd Hoopes, Zvi Kelman, David Travis Gallagher
The crystallizable fragment (Fc) domain of immunoglobulin subclass IgG1 antibodies is engineered for a wide variety of pharmaceutical applications. Two

SARS-CoV-2 infection establishes an enhanced, stable, and age-independent CD8+ T cell response against a dominant nucleocapsid epitope using highly restricted TCRs

Author(s)
Cecily Choy, Joseph Chen, Jiangyuan Li, Jian Lu, Daichao Wu, Ainslee Zou, Humza Hemani, Beverly Baptiste, Emily Wichmann, Qian Yang, Jeffrey Ciffelo, Rui Yin, Julia McKelvy, Denise Melvin, Tonya Wallace, Christopher Dunn, Cuong Nguyen, Chee Chia, Jingshui Fan, Jeannie Ruffolo, Linda Zukley, Guixin Shi, Tomokazu Amano, An Yang, Osorio Meirelles, Wells Wu, Rong-Fong Chen, RICHARD WILLIS, Minoru Ko, Y-T Liu, Supriyo De, Brian Pierce, Luigi Ferrucci, josephine egan, Roy Mariuzza, Nan-ping Weng, David Travis Gallagher
We analyzed circulating CD8+ T cells recognizing six epitopes from the SARS-CoV-2 nucleocapsid (N) protein in HLA-A2+ unexposed and recovered COVID-19 patients

Design and characterization of a protein fold switching network

Author(s)
David Travis Gallagher, Biao Ruan, Yanan He, Yingwei Chen, Eun Jung Choi, Yihong Chen, Dana Motabar, Tsega Solomon, Richard Simmerman, Thomas Kauffman, John Orban, Philip Bryan
Protein sequences encoding three common small folds (3-alpha, beta-grasp, and alpha/beta plait) were connected in a network of mutational pathways that
Created October 9, 2019, Updated July 2, 2025
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