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Response of Rubredoxin from Pyrococcus furiosus to Environmental Changes: Implications for the Origin of Hyperthermostability

Cite this: Biochemistry 1995, 34, 31, 9865–9873
Publication Date (Print):August 8, 1995
https://doi.org/10.1021/bi00031a007
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    3. Dong Hyun Jung,, Nam Sook Kang, and, Mu Shik Jhon. Site-Directed Mutation Study on Hyperthermostability of Rubredoxin from Pyrococcus furiosus Using Molecular Dynamics Simulations in Solution. The Journal of Physical Chemistry A 1997, 101 (4) , 466-471. https://doi.org/10.1021/jp9617940
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    6. Sanjeev Kumar Chandrayan, Satya Prakash, Shubbir Ahmed, Purnananda Guptasarma, . Hyperthermophile Protein Behavior: Partially-Structured Conformations of Pyrococcus furiosus Rubredoxin Monomers Generated through Forced Cold-Denaturation and Refolding. PLoS ONE 2014, 9 (3) , e80014. https://doi.org/10.1371/journal.pone.0080014
    7. Satya Prakash, Monica Sundd, Purnananda Guptasarma, . The Key to the Extraordinary Thermal Stability of P. furiosus Holo-Rubredoxin: Iron Binding-Guided Packing of a Core Aromatic Cluster Responsible for High Kinetic Stability of the Native Structure. PLoS ONE 2014, 9 (3) , e89703. https://doi.org/10.1371/journal.pone.0089703
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    42. Reinhard Sterner, Gerd R. Kleemann, Halina Szadkowski, Ariel Lustig, Kasper Kirschner, Michael Hennig. Phosphoribosyl anthranilate isomerase from Thermotoga maritima is an extremely stable and active homodimer. Protein Science 1996, 5 (10) , 2000-2008. https://doi.org/10.1002/pro.5560051006
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