Wassenberg, Doris and Welker, Christine and Jaenicke, Rainer (1999) Thermodynamics of the unfolding of the cold-shock protein from Thermotoga maritima. JOURNAL OF MOLECULAR BIOLOGY, 289 (1). pp. 187-193. ISSN 0022-2836, 1089-8638
Full text not available from this repository. (Request a copy)Abstract
Proteins from (hyper-)thermophiles are known to exhibit high intrinsic stabilities. Commonly, their thermodynamic characterization is impeded by irreversible side reactions of the thermal analysis or calorimetrical problems. Small single-domain proteins are suitable candidates to overcome these obstacles. Here, the thermodynamics of the thermal denaturation of the recombinant cold-shock protein (Csp) from the hyperthermophilic bacterium Thermotoga maritima (Tm) was studied by differential scanning calorimetry. The unfolding transition can be described over a broad pH range (3.5-8.5) by a reversible two-state process. Maximum stability (Delta G(25 degrees C) = 6.5 kcal/mol) was observed at pH 5-6 where TmCsp unfolds with a melting temperature at 95 degrees C. The heat capacity difference between the native and the denatured states is 1.1(+/- 0.1) kcal/(mol K). At pH 7, thermal denaturation occurs at 82 degrees C. The corresponding free energy profile has its maximum at 30 degrees C with Delta G(N --> U) = 4.8(+/-0.5) kcal/mol. At the optimal growth temperature of T. maritima (80 degrees C), TmCsp in the absence of ligands is only marginally stable, with a free energy of stabilization not far beyond the thermal energy. With the known stabilizing effect of nucleic acids in mind, this suggests a highly dynamical interaction of TmCsp with its target molecules. (C) 1999 Academic Press.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | BACILLUS-SUBTILIS; HYDROPHOBIC INTERACTION; HISTIDINE-RESIDUES; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; HEAT-CAPACITY; BINDING; RIBONUCLEASE-T1; DENATURATION; STABILITY; cold-shock protein; differential scanning calorimetry (DSC); hyperthermophiles; stability; Thermotoga maritima |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 10 Feb 2023 11:08 |
| Last Modified: | 10 Feb 2023 11:08 |
| URI: | https://pred.uni-regensburg.de/id/eprint/49238 |
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