2mdu | pdb_00002mdu
From Proteopedia
Circular Permutant of the WW Domain with Loop 1 Excised
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Structural highlights
Publication Abstract from PubMedA hyperstable Pin1 WW domain has been circularly permuted via excision of the fold-nucleating turn; it still folds to form the native three-strand sheet and hydrophobic core features. Multiprobe folding dynamics studies of the normal and circularly permuted sequences, as well as their constituent hairpin fragments and comparable-length beta-strand-loop-beta-strand models, indicate 2-state folding for all topologies. N-terminal hairpin formation is the fold nucleating event for the wild-type sequence; the slower folding circular permutant has a more distributed folding transition state. Circular Permutation of a WW Domain: Folding Still Occurs after Excising the Turn of the Folding-Nucleating Hairpin.,Kier BL, Anderson JM, Andersen NH J Am Chem Soc. 2014 Jan 3. PMID:24350581[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 11:55, 22 November 2023.