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Detection and Analysis of Chimeric Tertiary Structures by Backbone Thioester Exchange: Packing of an α Helix against an α/β‐Peptide Helix
Author(s) -
Price Joshua L.,
Hadley Erik B.,
Steinkruger Jay D.,
Gellman Samuel H.
Publication year - 2010
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200904714
Subject(s) - antiparallel (mathematics) , coiled coil , helix (gastropod) , protein tertiary structure , chemistry , crystallography , peptide , stereochemistry , biochemistry , physics , biology , ecology , quantum mechanics , snail , magnetic field
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.