On the extraordinary pressure stability of the Thermotoga maritima arginine binding protein and its folded fragments – a high-pressure FTIR spectroscopy study-Reference-Cited by-同舟云学术

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

Published:2020 Issue:20 Volume:22 Page:11244-11248
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Jaworek Michel W.¹²³⁴⁵,Ruggiero Alessia⁶⁷⁸⁹,Graziano Giuseppe¹⁰¹¹¹²⁹^ORCID,Winter Roland¹²³⁴⁵^ORCID,Vitagliano Luigi⁶⁷⁸⁹^ORCID

Affiliation:

1. Faculty of Chemistry and Chemical Biology

2. Biophysical Chemistry

3. TU Dortmund University

4. D-44227 Dortmund

5. Germany

6. Institute of Biostructures and Bioimaging

7. C. N. R

8. Naples

9. Italy

10. Department of Science and Technology

11. University of Sannio

12. Benevento

Abstract

The domain swapped dimer of the arginine binding protein from Thermotoga maritima and its truncated variants are stable even at 10 kbar of pressure.

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2020/CP/D0CP01618G

Reference33 articles.

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2. Protein oligomerization: How and why

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4. 3D domain swapping: As domains continue to swap

5. A structural classification of substrate-binding proteins

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