Loading...
Computational Design of Affinity and Specificity at Protein-Protein Interfaces
Karanicolas, John Kuhlman, Brian
Karanicolas, John
Kuhlman, Brian
Citations
Altmetric:
Abstract
The computer-based design of protein-protein interactions is a rigorous test of our understanding of molecular recognition and an attractive approach for creating novel tools for cell and molecular research. Considerable attention has been placed on redesigning the affinity and specificity of naturally occurring interactions. Several studies have shown that reducing the desolvation costs for binding while preserving shape complimentarity and hydrogen bonding is an effective strategy for improving binding affinities. In favorable cases specificity has been designed by focusing only on interactions with the target protein, while in cases with closely related off-target proteins, it has been necessary to explicitly disfavor unwanted binding partners. The rational design of protein-protein interactions from scratch is still an unsolved problem, but recent developments in flexible backbone design and energy functions hold promise for the future.
Description
Date
2009-08
Journal Title
Journal ISSN
Volume Title
Publisher
Elsevier
Collections
Research Projects
Organizational Units
Journal Issue
Keywords
Rational protein design, Computational protein design, De novo protein design, Protein-protein interactions
Citation
Karanicolas, J., & Kuhlman, B. (2009). Computational Design of Affinity and Specificity at Protein-Protein Interfaces. Current Opinion in Structural Biology, 19(4), 458–463. http://doi.org/10.1016/j.sbi.2009.07.005