Stabilization of hen egg white lysozyme by a cavity-filling mutation.


Abstract

Stabilization of a protein using cavity-filling strategy has hardly been successful because of unfavorable van der Waals contacts. We succeeded in stabilizing lysozymes by cavity-filling mutations. The mutations were checked by a simple energy minimization in advance. It was shown clearly that the sum of free energy change caused by the hydrophobicity and the cavity size was correlated very well with protein stability. We also considered the aromatic-aromatic interaction. It is reconfirmed that the cavity-filling mutation in a hydrophobic core is a very useful method to stabilize a protein when the mutation candidate is selected carefully. Study holds ProTherm entries: 10862, 10863, 10864, 10865, 10866, 14571, 14572, 14573, 14574 Extra Details: cavity-filling mutation; lysozyme; stability; aromatic-aromatic interaction

Submission Details

ID: fNZx72jC

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:41 p.m.

Version: 1

Publication Details
Ohmura T;Ueda T;Ootsuka K;Saito M;Imoto T,Protein Sci. (2001) Stabilization of hen egg white lysozyme by a cavity-filling mutation. PMID:11266617
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