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Thermodynamics of the unfolding of the cold-shock protein from Thermotoga maritima.
J Mol Biol. 1999 May 28; 289(1):187-93.JM

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 (DeltaG (25 degrees C)=6.5 kcal/mol) was observed at pH 5-6 where Tm Csp 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 DeltaGN-->U=4.8(+/-0.5) kcal/mol. At the optimal growth temperature of T. maritima (80 degrees C), Tm Csp 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 Tm Csp with its target molecules.

Authors+Show Affiliations

Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, Regensburg, D-93040, Germany.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

10339416

Citation

Wassenberg, D, et al. "Thermodynamics of the Unfolding of the Cold-shock Protein From Thermotoga Maritima." Journal of Molecular Biology, vol. 289, no. 1, 1999, pp. 187-93.
Wassenberg D, Welker C, Jaenicke R. Thermodynamics of the unfolding of the cold-shock protein from Thermotoga maritima. J Mol Biol. 1999;289(1):187-93.
Wassenberg, D., Welker, C., & Jaenicke, R. (1999). Thermodynamics of the unfolding of the cold-shock protein from Thermotoga maritima. Journal of Molecular Biology, 289(1), 187-93.
Wassenberg D, Welker C, Jaenicke R. Thermodynamics of the Unfolding of the Cold-shock Protein From Thermotoga Maritima. J Mol Biol. 1999 May 28;289(1):187-93. PubMed PMID: 10339416.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Thermodynamics of the unfolding of the cold-shock protein from Thermotoga maritima. AU - Wassenberg,D, AU - Welker,C, AU - Jaenicke,R, PY - 1999/5/26/pubmed PY - 1999/5/26/medline PY - 1999/5/26/entrez SP - 187 EP - 93 JF - Journal of molecular biology JO - J Mol Biol VL - 289 IS - 1 N2 - 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 (DeltaG (25 degrees C)=6.5 kcal/mol) was observed at pH 5-6 where Tm Csp 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 DeltaGN-->U=4.8(+/-0.5) kcal/mol. At the optimal growth temperature of T. maritima (80 degrees C), Tm Csp 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 Tm Csp with its target molecules. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/10339416/Thermodynamics_of_the_unfolding_of_the_cold_shock_protein_from_Thermotoga_maritima_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(99)92772-9 DB - PRIME DP - Unbound Medicine ER -