Exploring the energy landscape of antibody-antigen complexes: protein dynamics, flexibility, and molecular recognition
M.C. Thielges, J. Zimmermann, W. Yu, M. Oda, F.E. Romesberg, Biochemistry (2008) 47:7237-7247. [June 2008 Hot Article].
We examine a panel of antibodies elicited to the chromophoric antigen fluorescein. On the basis of isothermal titration calorimetry, we select six antibodies that bind fluorescein with diverse binding entropies, suggestive of varying contributions of dynamics to molecular recognition. We find that more than half of all the somatic mutations among the six antibodies are located in positions unlikely to contact fluorescein directly, and using 3PEPS and TG spectroscopy, we find a high level of dynamic diversity among the antibodies.