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Computational Design of Affinity and Specificity at Protein-Protein Interfaces

dc.contributor.authorKaranicolas, John
dc.contributor.authorKuhlman, Brian
dc.date.accessioned2017-06-08T19:19:25Z
dc.date.available2017-06-08T19:19:25Z
dc.date.issued2009-08
dc.identifier.citationKaranicolas, 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.2009.07.005en_US
dc.identifier.urihttp://hdl.handle.net/1808/24446
dc.description.abstractThe 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.en_US
dc.publisherElsevieren_US
dc.rightsThis is an open access article under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License 4.0 (CC BY-NC-ND 4.0), which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.en_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/en_US
dc.subjectRational protein designen_US
dc.subjectComputational protein designen_US
dc.subjectDe novo protein designen_US
dc.subjectProtein-protein interactionsen_US
dc.titleComputational Design of Affinity and Specificity at Protein-Protein Interfacesen_US
dc.typeArticleen_US
kusw.kuauthorKaranicolas, John
kusw.kudepartmentMolecular Biosciencesen_US
kusw.oanotesPer SHERPA/RoMEO 6/8/2017: Author's Pre-print: green tick author can archive pre-print (ie pre-refereeing) Author's Post-print: green tick author can archive post-print (ie final draft post-refereeing) Publisher's Version/PDF: cross author cannot archive publisher's version/PDF General Conditions:

Authors pre-print on any website, including arXiv and RePEC Author's post-print on author's personal website immediately Author's post-print on open access repository after an embargo period of between 12 months and 48 months Permitted deposit due to Funding Body, Institutional and Governmental policy or mandate, may be required to comply with embargo periods of 12 months to 48 months Author's post-print may be used to update arXiv and RepEC Publisher's version/PDF cannot be used Must link to publisher version with DOI Author's post-print must be released with a Creative Commons Attribution Non-Commercial No Derivatives License		en_US
dc.identifier.doi10.1016/j.sbi.2009.07.005en_US
kusw.oaversionScholarly/refereed, author accepted manuscripten_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US
dc.identifier.pmidPMC2882636en_US
dc.rights.accessrightsopenAccess


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This is an open access article under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License 4.0 (CC BY-NC-ND 4.0), which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.
Except where otherwise noted, this item's license is described as: This is an open access article under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License 4.0 (CC BY-NC-ND 4.0), which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.