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Article

Irreversible thermal denaturation of elongation factor Ts from Thermus thermophilus effect of the residual structure and intermonomer disulfide bond.

Biochimica et biophysica acta - 1 Jul 2006

Zoldák Gabriel, Sedlák Erik, Valusová Eva, Wolfrum Alexandra, Marek Jozef, Antalík Marián, Sprinzl Mathias

Abstract excerpt

The homodimeric wild-type elongation factor Ts, EF-Ts(wt), and its C190A mutant, EF-Ts(C190A), from Thermus thermophilus goes through thermal denaturation in a way consistent with a two state irreversible model with a relatively high activation energy, approximately 530 kJ/mol (Supplemental materials provides a list of 98 activation energies from 54 proteins in various solvent conditions). Removing the...

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PMID: 16781902
DOI: 10.1016/j.bbapap.2006.04.011

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

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