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Thermal denaturation of the core protein of lac repressor

Manly, Susan P., Matthews, Kathleen S., Sturtevant, Julian M.·1985·Biochemistry

Abstract

The thermal denaturation of the core protein of lac repressor was studied alone and in the presence of the inducer isopropyl beta-D-thiogalactoside (IPTG) and the antiinducer o-nitrophenyl beta-D-fucoside (ONPF) by means of high-sensitivity differential scanning calorimetry. The denaturation that takes place at about 65 degrees C is apparently irreversible; i.e., a rescan of a previously scanned sample of protein solution shows no denaturational endotherm. Despite this irreversibility, the denaturation appeared to follow quantitatively the dictates of equilibrium thermodynamics as embodied in the van't Hoff equation. The results obtained indicate clearly that the tetrameric protein dissociates to monomers during denaturation and that the ligands are not dissociated until denaturation takes place. The enthalpy of denaturation of the protein is 4.57 +/- 0.25 cal g-1 and is independent of temperature. The enthalpies of dissociation of IPTG and ONPF at the denaturation temperature are very large, 37 and 42 kcal (mol of ligand)-1, respectively.

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Metadata

Authors
Manly, S. P., Matthews, K. S., & Sturtevant, J. M.
Venue
Biochemistry
Published
1985-07-01
Volume
24
Issue
15
Pages
3842-3846
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
OpenAlex
W2089985532
Cited by
165
References
0
FWCI
8.13
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Thermal denaturation of the core protein of lac repressor. https://app.cochat.ai/papers/10.1021/bi00336a004
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Manly, S. P., Matthews, K. S., & Sturtevant, J. M. (1985). Thermal denaturation of the core protein of lac repressor. Biochemistry. https://doi.org/10.1021/bi00336a004

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