Thermal unfolding of monomeric and dimeric beta-lactoglobulins.
Abstract: The thermal stabilities of dimeric bovine beta-lactoglobulin and monomeric equine beta-lactoglobulin were investigated at neutral pH by means of differential scanning calorimetry, circular dichroism, tryptophan fluorescence, and by binding of an hydrophobic probe. Differential scanning calorimetry showed the presence of two structural domains with different thermal stabilities in both proteins. Thermodynamic analysis of the calorimetric signal revealed that the two domains unfold independently according to a mechanism where an equilibrium step is followed by an irreversible transition. The spectroscopic data supported this model and allowed recognition of the structural regions corresponding to the more thermally stable domain. The differences in thermal stability between the two proteins can be primarily ascribed to the properties of the less stable domain.
Publication Date: 2001-10-19 PubMed ID: 11606207DOI: 10.1046/j.0014-2956.2001.02484.xGoogle Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research article investigates the thermal stability of monomeric equine beta-lactoglobulin and dimeric bovine beta-lactoglobulin, discovering distinct thermal stabilities across two structural domains.
Overview
- This research investigates the thermal stability of two proteins, dimeric bovine beta-lactoglobulin and monomeric equine beta-lactoglobulin, at neutral pH levels. These proteins were analyzed using various scientific techniques such as differential scanning calorimetry, circular dichroism, tryptophan fluorescence and the use of a hydrophobic probe.
Thermal Stability of Protein Structures
- The research identified two structural domains with different thermal stabilities in both proteins. A structural domain in this context refers to a segment of the protein that can independently fold into a stable structure.
- Differential scanning calorimetry was used to identify these domains. This technique measures the amount of energy absorbed or released by a sample when it’s heated or cooled, providing insights into the structural stability of the proteins.
Thermodynamic Analysis
- Upon analyzing the calorimetric signal through a thermodynamic lens, it was observed that these two domains unfold independently, suggesting varying levels of stability across the protein structure. This unfolding mechanism was characterized by an equilibrium step—where the system is stable and changes are reversible—followed by an irreversible transition—where changes in the protein structure become permanent.
Spectroscopic Data
- Spectroscopic data, obtained through techniques like circular dichroism and tryptophan fluorescence, supported the proposed model of domain unfolding. Further, these techniques allowed the researchers to identify the specific structural regions corresponding to the more thermally stable domain.
Comparative Stability
- In comparing the two proteins, it was found that the differences in their thermal stability can be mostly attributed to the properties of the less stable domain. This finding suggests a key role for these less stable domains in determining the characteristics and behavior of these proteins.
Cite This Article
APA
Fessas D, Iametti S, Schiraldi A, Bonomi F.
(2001).
Thermal unfolding of monomeric and dimeric beta-lactoglobulins.
Eur J Biochem, 268(20), 5439-5448.
https://doi.org/10.1046/j.0014-2956.2001.02484.x Publication
Researcher Affiliations
- Calorimetry Laboratory, DISTAM, Section of Food Technology, Milan, Italy. Dimitrios.Fessas@unimi.it
MeSH Terms
- Animals
- Calorimetry, Differential Scanning
- Cattle
- Circular Dichroism
- Dimerization
- Horses
- Lactoglobulins / chemistry
- Lactoglobulins / metabolism
- Protein Denaturation
- Protein Folding
- Protein Structure, Quaternary
- Protein Structure, Tertiary
- Spectrometry, Fluorescence
- Temperature
- Thermodynamics
- Tryptophan / chemistry
Citations
This article has been cited 16 times.- Barbiroli A, Iametti S, Bonomi F. Beta-Lactoglobulin as a Model Food Protein: How to Promote, Prevent, and Exploit Its Unfolding Processes.. Molecules 2022 Feb 8;27(3).
- Jin R, Grasso M, Zhou M, Marmorstein R, Baumgart T. Unfolding Mechanisms and Conformational Stability of the Dimeric Endophilin N-BAR Domain.. ACS Omega 2021 Aug 17;6(32):20790-20803.
- Pelosi C, Duce C, Wurm FR, Tinè MR. Effect of Polymer Hydrophilicity and Molar Mass on the Properties of the Protein in Protein-Polymer Conjugates: The Case of PPEylated Myoglobin.. Biomacromolecules 2021 May 10;22(5):1932-1943.
- Barreto ÍMLG, Urbano SA, Oliveira CAA, Macêdo CS, Borba LHF, Chags BME, Rangel AHN. Chemical composition and lipid profile of mare colostrum and milk of the quarter horse breed.. PLoS One 2020;15(9):e0238921.
- Coltelli MB, Aliotta L, Gigante V, Bellusci M, Cinelli P, Bugnicourt E, Schmid M, Staebler A, Lazzeri A. Preparation and Compatibilization of PBS/Whey Protein Isolate Based Blends.. Molecules 2020 Jul 21;25(14).
- Lighezan L, Georgieva R, Neagu A. The secondary structure and the thermal unfolding parameters of the S-layer protein from Lactobacillus salivarius.. Eur Biophys J 2016 Sep;45(6):491-509.
- Tsitsanou KE, Drakou CE, Thireou T, Vitlin Gruber A, Kythreoti G, Azem A, Fessas D, Eliopoulos E, Iatrou K, Zographos SE. Crystal and solution studies of the "Plus-C" odorant-binding protein 48 from Anopheles gambiae: control of binding specificity through three-dimensional domain swapping.. J Biol Chem 2013 Nov 15;288(46):33427-38.
- Silva I, Sansone S, Brancaleon L. An anionic porphyrin binds beta-lactoglobulin A at a superficial site rich in lysine residues.. Protein J 2009 Jan;28(1):1-13.
- Saadati Z, Bordbar AK. Stability of beta-lactoglobulin A in the presence of sugar osmolytes estimated from their guanidinium chloride-induced transition curves.. Protein J 2008 Dec;27(7-8):455-60.
- Fernandez NF, Sansone S, Mazzini A, Brancaleon L. Irradiation of the porphyrin causes unfolding of the protein in the protoporphyrin IX/beta-lactoglobulin noncovalent complex.. J Phys Chem B 2008 Jun 26;112(25):7592-600.
- Bromley EH, Krebs MR, Donald AM. Mechanisms of structure formation in particulate gels of beta-lactoglobulin formed near the isoelectric point.. Eur Phys J E Soft Matter 2006 Oct;21(2):145-52.
- Lozinsky E, Iametti S, Barbiroli A, Likhtenshtein GI, Kálai T, Hideg K, Bonomi F. Structural features of transiently modified beta-lactoglobulin relevant to the stable binding of large hydrophobic molecules.. Protein J 2006 Jan;25(1):1-15.
- Yesylevskyy SO, Kharkyanen VN, Demchenko AP. Dynamic protein domains: identification, interdependence, and stability.. Biophys J 2006 Jul 15;91(2):670-85.
- Croguennec T, Mollé D, Mehra R, Bouhallab S. Spectroscopic characterization of heat-induced nonnative beta-lactoglobulin monomers.. Protein Sci 2004 May;13(5):1340-6.
- Bonomi F, Eidsness MK, Iametti S, Kurtz DM Jr, Mazzini S, Morleo A. Contribution of the [FeII(SCys)4] site to the thermostability of rubredoxins.. J Biol Inorg Chem 2004 Apr;9(3):297-306.
- Pollegioni L, Iametti S, Fessas D, Caldinelli L, Piubelli L, Barbiroli A, Pilone MS, Bonomi F. Contribution of the dimeric state to the thermal stability of the flavoprotein D-amino acid oxidase.. Protein Sci 2003 May;12(5):1018-29.
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