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Issue 20, 2020
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On the extraordinary pressure stability of the Thermotoga maritima arginine binding protein and its folded fragments – a high-pressure FTIR spectroscopy study

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Abstract

The arginine binding protein from T. maritima (ArgBP) exhibits several distinctive biophysical and structural properties. Here we show that ArgBP is also endowed with a ramarkable pressure stability as it undergoes minor structural changes only, even at 10 kbar. A similar stability is also observed for its folded fragments (truncated monomer and individual domains). A survey of literature data on the pressure stability of proteins highlights the uncommon behavior of ArgBP.

Graphical abstract: On the extraordinary pressure stability of the Thermotoga maritima arginine binding protein and its folded fragments – a high-pressure FTIR spectroscopy study

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Article information


Submitted
25 Mar 2020
Accepted
04 May 2020
First published
04 May 2020

Phys. Chem. Chem. Phys., 2020,22, 11244-11248
Article type
Communication

On the extraordinary pressure stability of the Thermotoga maritima arginine binding protein and its folded fragments – a high-pressure FTIR spectroscopy study

M. W. Jaworek, A. Ruggiero, G. Graziano, R. Winter and L. Vitagliano, Phys. Chem. Chem. Phys., 2020, 22, 11244
DOI: 10.1039/D0CP01618G

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