Peptide backbone circularization enhances antifreeze protein thermostability

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Backbone circularization of Bacillus subtilis family 11 xylanase increases its thermostability and its resistance against aggregation.

The activity of proteins is dictated by their three-dimensional structure, the native state, and is influenced by their ability to remain in or return to the folded native state under physiological conditions. Backbone circularization is thought to increase protein stability by decreasing the conformational entropy in the unfolded state. A positive effect of circularization on stability has bee...

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ژورنال

عنوان ژورنال: Protein Science

سال: 2017

ISSN: 0961-8368

DOI: 10.1002/pro.3228