Engineering Enzyme Stability and Resistance to an Organic Cosolvent by Modification of Residues in the Access Tunnel

Abstract

Mutationen von vier Resten entlang des Zugangstunnels verlängerten die Halbwertzeit eines Enzyms in 40 % Dimethylsulfoxid von Minuten zu Wochen und erhöhten die Schmelztemperatur um 19 °C. Proteinkristallographie und Moleküldynamik zeigen, dass die Packung der Tunnelreste entscheidend für die Proteinstabilität und die Zugänglichkeit des aktiven Zentrums für Cosolvens-Moleküle (rote Punkte) ist. As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.