Detection and Analysis of Chimeric Tertiary Structures by Backbone Thioester Exchange: Packing of an α Helix against an α/β-Peptide Helix

Backbone thioester exchange is used to explore a fundamental type of protein–foldamer packing motif, the association of an α helix and an α/β‐peptide foldameric helix, which is analogous to an antiparallel coiled‐coil tertiary structure in a pure α‐residue backbone. Side‐chain packing preferences at...

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Published in:Angewandte Chemie (International ed.) Vol. 49; no. 2; pp. 368 - 371
Main Authors: Price, Joshua L, Hadley, Erik B, Steinkruger, Jay D, Gellman, Samuel H
Format: Journal Article
Language:English
Published: Weinheim Wiley-VCH Verlag 01-01-2010
WILEY-VCH Verlag
WILEY‐VCH Verlag
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Summary:Backbone thioester exchange is used to explore a fundamental type of protein–foldamer packing motif, the association of an α helix and an α/β‐peptide foldameric helix, which is analogous to an antiparallel coiled‐coil tertiary structure in a pure α‐residue backbone. Side‐chain packing preferences at this chimeric tertiary interface are comparable to those that determine pairing propensities among antiparallel α helices.
Bibliography:http://dx.doi.org/10.1002/anie.200904714
ark:/67375/WNG-94LWD1D1-5
NIH - No. GM-61238; No. T32 GM008505
istex:D9DC7F15351AB6BEDCB07388E143E6090CA509B2
This research was supported by the NIH Grant GM-61238. J.L.P. was supported in part by an NIH Chemical Biology Training Grant (T32 GM008505). We thank Dr. Darrell McCaslin for assistance with AU experiments, and Peptech for providing β3-amino acids at a discounted price.
ArticleID:ANIE200904714
This research was supported by the NIH Grant GM‐61238. J.L.P. was supported in part by an NIH Chemical Biology Training Grant (T32 GM008505). We thank Dr. Darrell McCaslin for assistance with AU experiments, and Peptech for providing β
3
These authors contributed equally.
amino acids at a discounted price.
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ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200904714