Published March 21, 2011
| Accepted Version
Journal Article
Open
Homoisoleucine: A Translationally Active Leucine Surrogate of Expanded Hydrophobic Surface Area
Abstract
Hil of a strong peptide! Homoisoleucine (Hil) serves as an effective surrogate for leucine with respect to protein translation in bacterial cells. Replacement of Leu by Hil stabilizes coiled-coil peptides, as shown by the elevation of the thermal denaturation temperature. The increase in denaturation temperature is larger than that observed previously for replacement of Leu by trifluoroleucine.
Additional Information
© 2011 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. Received: December 9, 2010; Published online on February 15, 2011. We thank Shelly Tzlil for assistance in implementing the model for thermal unfolding of coiled-coil peptides in Matlab. This research was supported by NIH grant GM62523. J.A.V. was supported in part by an N.D.S.E.G. Fellowship; J.D.F. was supported in part by an NIH Postdoctoral Fellowship.Attached Files
Accepted Version - nihms312366.pdf
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Additional details
- PMCID
- PMC3149977
- Eprint ID
- 23237
- Resolver ID
- CaltechAUTHORS:20110404-112939537
- GM62523
- NIH
- National Defense Science and Engineering Graduate (NDSEG) Fellowship
- NIH Postdoctoral Fellowship
- Created
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2011-04-04Created from EPrint's datestamp field
- Updated
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2021-11-09Created from EPrint's last_modified field