The Zero-Order Loop in Apoazurin Modulates Folding Mechanism In Silico
Abstract
Pseudomonas aeruginosa apoazurin (apo, without the copper cofactor) has a single disulfide bond between residues 3 and 26 and unfolds in a two-state reaction in vitro. The disulfide bond covalently connects the N-termini of β-strands 1 and 3; thereby, it creates a zero-order loop or a “cinch” that restricts conformational space. Covalent loops and threaded topologies are emerging as important structural elements in folded proteins and may be...
Paper Details
Title
The Zero-Order Loop in Apoazurin Modulates Folding Mechanism In Silico
Published Date
Apr 5, 2021
Volume
125
Issue
14
Pages
3501 - 3509
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