Evidence of a two-stage thermal denaturation process in lysozyme: A Raman scattering and differential scanning calorimetry investigation
Evidence of a two-stage thermal denaturation process in lysozyme: A Raman scattering and differential scanning calorimetry investigation
Engineering Village 2
? 2006 Elsevier Inc
Accession number: 8727663
Title: Evidence of a two-stage thermal denaturation process in lysozyme: A Raman scattering and differential scanning calorimetry investigation
Authors: Hedoux, A.1 ; Ionov, R.; Willart, J.-F.; Lerbret, A.; Affouard, F.; Guinet, Y.; Descamps, M.; Prevost, D.; Paccou, L.; Danede, F.
Author affiliation: 1 Lab. de Dynamique et Struct. des Mater. Moleculaires, UMR CNRS, Villeneuve d'Ascq, France
Serial title: Journal of Chemical Physics
Abbreviated serial title: J. Chem. Phys. (USA)
Volume: 124
Issue: 1
Publication date: 7 Jan. 2006
Pages: 14703-1-7
Language: English
ISSN: 0021-9606
CODEN: JCPSA6
Document type: Journal article (JA)
Publisher: AIP
Country of publication: USA
Material Identity Number: J008-2006-006
Abstract: Raman spectroscopy (in the low-frequency range and the amide I band region) and modulated differential scanning calorimetry investigations have been used to analyze temperature-induced structural changes in lysozyme dissolved in 1H2O and 2H2O in the thermal denaturation process. Low-frequency Raman data reveal a change in tertiary structure without concomitant unfolding of the secondary structure. Calorimetric data show that this structural change is responsible for the configurational entropy change associated with the strong-to-fragile liquid transition and correspond to about 1/3 of the native-denaturated transition enthalpy. This is the first stage of the thermal denaturation which is a precursor of the secondary structure change and is determined to be strongly dependent on the stability of the hydrogen-bond network in water. Low-frequency Raman spectroscopy provides information on the flexibility of the tertiary structure (in the native state and the transient folding state) in relation to the fragility of the mixture. The unfolding of the secondary structure appears as a consequence of the change in the tertiary structure and independent of the solvent. Protein conformational stability is directly dependent on the stability of the native tertiary structure. The structural transformation of tertiary structure can be detected through the enhanced 1H/2H exchange inhibited in native proteins. Taking into account similar features reported in the literature observed for different proteins it can be considered that the two-stage transformation observed in lysozyme dissolved in water is a general mechanism for the thermal denaturation of proteins
Number of references: 24
Inspec controlled terms: biothermics - differential scanning calorimetry - enthalpy - entropy - enzymes - hydrogen bonds - Raman spectra - solid-state phase transformations
Uncontrolled terms: two-stage thermal denaturation process - temperature-induced lysozyme structure - Raman scattering - modulated differential scanning calorimetry - Raman spectroscopy - amide I band region - 1H2O - 2H2O - low-frequency Raman data - native tertiary structure - concomitant unfolding - secondary structure - configurational entropy - strong-to-fragile liquid transition - native-denaturated transition enthalpy - hydrogen-bond network stability - water - transient folding state - native protein conformational stability - tertiary structural transformation - enhanced 1H-2H exchange - two-stage transformation
Inspec classification codes: A8715M Interactions with radiations at the biomolecular level - A8715B Biomolecular structure, configuration, conformation, and active sites - A8716 Biothermics
Treatment: Experimental (EXP)
Discipline: Physics (A)
DOI: 10.1063/1.2139087
Database: Inspec
Copyright 2006, IEE
This is a subscription site. You will need to subscribe to Engineering Village 2 to view the details.
Votes:40
Comments: 0