EFFECT OF HIGH TEMPERATURE ON PROTEINASE K CRYSTALLIZATION PREDICTED BY MOLECULAR DYNAMICS

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Abstract

Molecular dynamics simulations revealed a notable thermal stability of the precursor cluster of proteinase K crystals (a dimer formed prior to crystallization) within the 20–60°C temperature range. This finding led to the hypothesis that crystallization at an atypically elevated temperature (50–60°C) could be feasible. This theoretical prediction was subsequently confirmed experimentally: proteinase K crystals were successfully grown after incubation at 60°C. The results not only demonstrate the predictive power of the molecular dynamics approach employed here for identifying optimal protein crystallization conditions, but also open new opportunities for capturing the catalytically relevant conformation of proteinase K.

About the authors

Yu. V Kordonskaya

National Research Centre "Kurchatov Institute"

Email: yukord@mail.ru
Moscow, Russia

A. S Ustinova

National Research Centre "Kurchatov Institute"

Moscow, Russia

K. V Tikhonova

National Research Centre "Kurchatov Institute"

Moscow, Russia

S. Yu Silvestrova

Loginov Moscow Clinical Scientific Center

Moscow, Russia

M. A Marchenkova

National Research Centre "Kurchatov Institute"; Southern Federal University

Moscow, Russia; Rostov-on-Don, Russia

Yu. V Pisarevsky

National Research Centre "Kurchatov Institute"

Moscow, Russia

Yu. A Dyakova

National Research Centre "Kurchatov Institute"

Moscow, Russia

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