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Title 

Molecular dynamics simulation integrating study for Cr3+-binding to arginine kinase

Authors 

Y X SiX X GuY CaiS J YinJ M YangY D ParkJinhyuk LeeG Y Qian

Publisher 

Elsevier

Issue Date 

2015

Citation 

Process Biochemistry, vol. 50, no. 9, pp. 1363-1371

Keywords 

AggregationArginine kinaseCr3+MD simulation

Abstract 

We simulated the 3D structure of arginine kinase from Exopalaemon carinicauda (ECAK) on the basis of homology modeling. Computational molecular dynamics simulations between ECAK and Cr3+ were conducted to elucidate the functional role of Cr3+ on ECAK structure and catalysis. As a result, the binding mechanism of Cr3+ to ECAK along with binding sites and structural changes were predicted. To confirm the simulation results, kinetic studies of Cr3+-mediated aggregation of ECAK were subsequently conducted. We found that Cr3+ significantly induced ECAK aggregation with a multi-phase kinetic process at a high dose of Cr3+. The spectrofluorimetric results showed that Cr3+-induced tertiary structural changes in ECAK caused extensive exposure of hydrophobic surfaces, which could be a triggering factor for inducing ECAK aggregation. Our study provides new information concerning the effect of Cr3+ on ECAK's enzymatic function and unfolding, including aggregation, which might be toxic or act as a negative regulator.

ISSN 

0032-9592

Link 

http://dx.doi.org/10.1016/j.procbio.2015.05.026

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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