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Structure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein design

Strop, Pavel and Marinescu, Andrei M. and Mayo, Stephen L. (2000) Structure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein design. Protein Science, 9 (7). pp. 1391-1394. ISSN 0961-8368. http://resolver.caltech.edu/CaltechAUTHORS:20110620-160435792

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Abstract

Six helix surface positions of protein G (Gβ1) were redesigned using a computational protein design algorithm, resulting in the five fold mutant Gβ1m2. Gβ1m2 is well folded with a circular dichroism spectrum nearly identical to that of Gβ1, and a melting temperature of 91 °C, ~6 °C higher than that of Gβ1. The crystal structure of Gβ1m2 was solved to 2.0 Å resolution by molecular replacement. The absence of hydrogen bond or salt bridge interactions between the designed residues in Gβ1m2 suggests that the increased stability of Gβ1m2 is due to increased helix propensity and more favorable helix dipole interactions.


Item Type:Article
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URLURL TypeDescription
http://dx.doi.org/10.1110/ps.9.7.1391DOIUNSPECIFIED
http://onlinelibrary.wiley.com/doi/10.1110/ps.9.7.1391/abstractPublisherUNSPECIFIED
Contact Email Address:steve@mayo.caltech.edu
Additional Information:© 2000 The Protein Society. Received March 29, 2000; Final Revision May 3, 2000; Accepted May 11, 2000. Article first published online: 31 Dec. 2008. This work was supported by the Howard Hughes Medical Institute (S.L.M.) and a NSF fellowship (P.S.).
Funders:
Funding AgencyGrant Number
Howard Hughes Medical Institute (HHMI)UNSPECIFIED
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Subject Keywords:Hydrogen Bonding, Crystallography: X-Ray, Static Electricity, Mutation, Models: Molecular, Algorithms, Protein Conformation, Protein Engineering, Nerve Tissue Proteins
Non-Subject Keywords:helix dipole interaction; helix propensity; protein design; protein G
Record Number:CaltechAUTHORS:20110620-160435792
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20110620-160435792
Official Citation:Strop, P., Marinescu, A. M. and Mayo, S. L. (2000), Structure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein design. Protein Science, 9: 1391–1394. doi: 10.1110/ps.9.7.1391
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:24136
Collection:CaltechAUTHORS
Deposited By: Marie Ary
Deposited On:21 Jun 2011 21:39
Last Modified:23 Aug 2016 10:02

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