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SYMMETRIC PROTEIN ARCHITECTURE IN PROTEIN DESIGN: TOP-DOWN SYMMETRIC DECONSTRUCTION

Title: Symmetric Protein Architecture in Protein Design.
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Name(s): Longo, Liam, author
Blaber, Michael, author
Type of Resource: text
Genre: text
Date Issued: 2014-08-20
Physical Form: computer
Physical Form: online resource
Extent: 1 online resource
Language(s): English
Abstract/Description: Top-down symmetric deconstruction (TDSD) is a joint experimental and computational approach to generate a highly stable, functionally benign protein scaffold for intended application in subsequent functional design studies. By focusing on symmetric protein folds, TDSD can leverage the dramatic reduction in sequence space achieved by applying a primary structure symmetric constraint to the design process. Fundamentally, TDSD is an iterative symmetrization process, in which the goal is to maintain or improve properties of thermodynamic stability and folding cooperativity inherent to a starting sequence (the “proxy”). As such, TDSD does not attempt to solve the inverse protein folding problem directly, which is computationally intractable. The present chapter will take the reader through all of the primary steps of TDSD--selecting a proxy, identifying potential mutations, establishing a stability/folding cooperativity screen--relying heavily on a successful TDSD solution for the common β-trefoil fold.
Identifier: FSU_libsubv1_scholarship_submission_1456502653 (IID), 10.1007/978-1-4939-1486-9_8 (DOI)
Keywords: Symmetric protein design, protein folding, protein engineering, phi-value analysis, β-trefoil, protein evolution
Persistent Link to This Record: http://purl.flvc.org/fsu/fd/FSU_libsubv1_scholarship_submission_1456502653
Owner Institution: FSU
Is Part Of: Methods in Molecular Biology.
Issue: vol. 1216

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Longo, L., & Blaber, M. (2014). Symmetric Protein Architecture in Protein Design. Methods In Molecular Biology. Retrieved from http://purl.flvc.org/fsu/fd/FSU_libsubv1_scholarship_submission_1456502653