Computational Design of Affinity and Specificity at Protein-Protein Interfaces
dc.contributor.author | Karanicolas, John | |
dc.contributor.author | Kuhlman, Brian | |
dc.date.accessioned | 2017-06-08T19:19:25Z | |
dc.date.available | 2017-06-08T19:19:25Z | |
dc.date.issued | 2009-08 | |
dc.identifier.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 | en_US |
dc.identifier.uri | http://hdl.handle.net/1808/24446 | |
dc.description.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. | en_US |
dc.publisher | Elsevier | en_US |
dc.rights | 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. | en_US |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | en_US |
dc.subject | Rational protein design | en_US |
dc.subject | Computational protein design | en_US |
dc.subject | De novo protein design | en_US |
dc.subject | Protein-protein interactions | en_US |
dc.title | Computational Design of Affinity and Specificity at Protein-Protein Interfaces | en_US |
dc.type | Article | en_US |
kusw.kuauthor | Karanicolas, John | |
kusw.kudepartment | Molecular Biosciences | en_US |
kusw.oanotes | Per 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.doi | 10.1016/j.sbi.2009.07.005 | en_US |
kusw.oaversion | Scholarly/refereed, author accepted manuscript | en_US |
kusw.oapolicy | This item meets KU Open Access policy criteria. | en_US |
dc.identifier.pmid | PMC2882636 | en_US |
dc.rights.accessrights | openAccess |
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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.