Campus Units

Biochemistry, Biophysics and Molecular Biology, Roy J. Carver Department of, Bioinformatics and Computational Biology, Baker Center for Bioinformatics and Biological Statistics

Document Type


Publication Version

Published Version

Publication Date


Journal or Book Title

Immunome Research





First Page



Motions of the IgG structure are evaluated using normal mode analysis of an elastic network model to detect hinges, the dominance of low frequency modes, and the most important internal motions. One question we seek to answer is whether or not IgG hinge motions facilitate antigen binding. We also evaluate the protein crystal and packing effects on the experimental temperature factors and disorder predictions. We find that the effects of the protein environment on the crystallographic temperature factors may be misleading for evaluating specific functional motions of IgG. The extent of motion of the antigen binding domains is computed to show their large spatial sampling. We conclude that the IgG structure is specifically designed to facilitate large excursions of the antigen binding domains. Normal modes are shown as capable of com- putationally evaluating the hinge motions and the spatial sampling by the structure. The antigen binding loops and the major hinge appear to behave similarly to the rest of the structure when we consider the dominance of the low frequency modes and the extent of internal motion. The full IgG structure has a lower spectral dimension than individual Fab domains, pointing to more efficient information transfer through the antibody than through each domain. This supports the claim that the IgG structure is specifically constructed to facilitate antigen binding by coupling motion of the antigen binding loops with the large scale hinge motions.


This article is published as Zimmermann MT, Skliros A, Kloczkowski A, Jernigan RL. Immunoglobulin structure exhibits control over CDR motion. Immunome Res 2011; 7:5 Posted with permission.

Creative Commons License

Creative Commons Attribution 4.0 License
This work is licensed under a Creative Commons Attribution 4.0 License.

Copyright Owner

Zimmermann et al



File Format