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

Price Joshua L. | Zendy; Hadley Erik B. | Zendy; Steinkruger Jay D. | Zendy; Gellman Samuel H. | Zendy

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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.

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