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• W2072420936 abstract "We have cyclized the polypeptide backbone of β‐lactamase with a short peptide loop as a novel method for protein stabilization, using intein‐mediated protein ligation. Successful cyclization was proven by mass spectrometry and subsequent re‐linearization by proteolytic cleavage, as well as by resistance against carboxypeptidase. Under the conditions of the experiment, no disulfide bond is present. The circular form of β‐lactamase was found to be significantly more stable against irreversible aggregation upon heating than the linear form. The circular form could be purified from the linear one either by this heat treatment or by a his‐tag which became exopeptidase‐resistant by cyclization. The increased stability of the circular form is probably due to the decreased conformational entropy in the unfolded state and in the intermediate states. While the introduction of additional disulfide bonds for protein stabilization follows the same rationale, the cyclization strategy may disturb the structure less and thus constitute a general method for stabilizing those proteins with N‐ and C‐termini in close proximity." @default.
• W2072420936 created "2016-06-24" @default.
• W2072420936 creator A5070551735 @default.
• W2072420936 creator A5083658123 @default.
• W2072420936 date "1999-10-05" @default.
• W2072420936 modified "2023-10-18" @default.
• W2072420936 title "Circular β‐lactamase: stability enhancement by cyclizing the backbone" @default.
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• W2072420936 doi "https://doi.org/10.1016/s0014-5793(99)01220-x" @default.
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