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Ferredoxin from the hyperthermophile Thermotoga maritima is stable beyond the boiling point of water.

Pfeil, W. and Gesierich, U. and Kleemann, G. R. and Sterner, Reinhard (1997) Ferredoxin from the hyperthermophile Thermotoga maritima is stable beyond the boiling point of water. Journal of molecular biology 272 (4), pp. 591-6.

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Abstract

Heat-stable proteins from hyperthermophilic microorganisms are ideally suited for investigating protein stability and evolution. We measured with differential scanning calorimetry and optical absorption spectroscopy the thermal stability of [4Fe-4S] ferredoxin from Thermotoga maritima (tfdx), which is a small electron transfer protein. The results are consistent with two-state unfolding at the ...

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Item Type:Article
Date:1997
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Identification Number:
ValueType
9325114PubMed ID
10.1006/jmbi.1997.1278DOI
Classification:
NotationType
Calorimetry, Differential ScanningMESH
Ferredoxins/chemistryMESH
Gram-Negative Anaerobic Straight, Curved, and Helical Rods/chemistryMESH
Hot TemperatureMESH
Protein FoldingMESH
Water/chemistryMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Owner: Universitätsbibliothek Regensburg
Deposited On:22 Mar 2010 09:13
Last Modified:22 Mar 2010 09:52
Item ID:13707
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