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Role of entropy in protein thermostability: folding kinetics of a hyperthermophilic cold shock protein at high temperatures using ¹⁹F NMR

Schuler, Benjamin and Kremer, Werner and Kalbitzer, Hans Robert and Jaenicke, Rainer (2002) Role of entropy in protein thermostability: folding kinetics of a hyperthermophilic cold shock protein at high temperatures using ¹⁹F NMR. Biochemistry 41 (39), pp. 11670-11680.

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Abstract

We used (19)F NMR to extend the temperature range accessible to detailed kinetic and equilibrium studies of a hyperthermophilic protein. Employing an optimized incorporation strategy, the small cold shock protein from the bacterium Thermotoga maritima (TmCsp) was labeled with 5-fluorotryptophan. Although chaotropically induced unfolding transitions revealed a significant decrease in the ...

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Item Type:Article
Date:2002
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
12269809PubMed ID
Classification:
NotationType
Bacterial Proteins/chemistryMESH
Calorimetry, Differential ScanningMESH
Carrier Proteins/chemistryMESH
EntropyMESH
Fluorine/chemistryMESH
Guanidine/chemistryMESH
Heat-Shock Proteins/chemistryMESH
Hot TemperatureMESH
KineticsMESH
Nuclear Magnetic Resonance, Biomolecular/methodsMESH
Protein DenaturationMESH
Protein FoldingMESH
Spectrometry, FluorescenceMESH
SpectrophotometryMESH
Thermotoga maritima/chemistryMESH
Tryptophan/chemistryMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:15 Sep 2010 09:15
Last Modified:15 Sep 2010 09:15
Item ID:16585
Owner Only: item control page
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