Literature DB >> 7813479

A model for the denaturation and aggregation of beta-lactoglobulin.

S P Roefs1, K G De Kruif.   

Abstract

A quantitatively correct kinetic model for the temperature-induced denaturation and aggregation of beta-lactoglobulin is presented. The model recognizes an initiation, a propagation and a termination step by analogy with polymer radical chemistry. The decrease in native beta-lactoglobulin is predicted to follow order 3/2, in agreement with experimental results. The size of the protein polymer particles is predicted to be proportional to the square root of the initial beta-lactoglobulin concentration. The scattered light intensity is proportional to the product of concentration and size of the protein polymer particles. The initial increase in scattering intensity of the particles therefore scales with the initial squared beta-lactoglobulin concentration. The influence of other reaction conditions, e.g. ionic strength and pH, can be incorporated via the reaction constants of the reaction kinetic pathway.

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Year:  1994        PMID: 7813479     DOI: 10.1111/j.1432-1033.1994.00883.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  14 in total

1.  Characterization and isolation of intermediates in beta-lactoglobulin heat aggregation at high pH.

Authors:  R Bauer; R Carrotta; C Rischel; L Ogendal
Journal:  Biophys J       Date:  2000-08       Impact factor: 4.033

2.  Heat-induced denaturation and aggregation of ovalbumin at neutral pH described by irreversible first-order kinetics.

Authors:  Mireille Weijers; Peter A Barneveld; Martien A Cohen Stuart; Ronald W Visschers
Journal:  Protein Sci       Date:  2003-12       Impact factor: 6.725

3.  Structural changes of beta-lactoglobulin during thermal unfolding and refolding--an FT-IR and circular dichroism study.

Authors:  C Bhattacharjee; S Saha; A Biswas; M Kundu; L Ghosh; K P Das
Journal:  Protein J       Date:  2005-01       Impact factor: 2.371

4.  Mechanisms of structure formation in particulate gels of beta-lactoglobulin formed near the isoelectric point.

Authors:  E H C Bromley; M R H Krebs; A M Donald
Journal:  Eur Phys J E Soft Matter       Date:  2006-12-07       Impact factor: 1.890

5.  Protein particulates: another generic form of protein aggregation?

Authors:  Mark R H Krebs; Glyn L Devlin; A M Donald
Journal:  Biophys J       Date:  2006-11-17       Impact factor: 4.033

6.  Amyloid fibril-like structure underlies the aggregate structure across the pH range for beta-lactoglobulin.

Authors:  Mark R H Krebs; Glyn L Devlin; Athene M Donald
Journal:  Biophys J       Date:  2009-06-17       Impact factor: 4.033

7.  Effect of temperature on the secondary structure of beta-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis.

Authors:  X L Qi; C Holt; D McNulty; D T Clarke; S Brownlow; G R Jones
Journal:  Biochem J       Date:  1997-05-15       Impact factor: 3.857

Review 8.  Dissociative mechanism for irreversible thermal denaturation of oligomeric proteins.

Authors:  Natalia A Chebotareva; Svetlana G Roman; Boris I Kurganov
Journal:  Biophys Rev       Date:  2016-10-17

9.  The self-association and thermal denaturation of caprine and bovine β-lactoglobulin.

Authors:  Jennifer M Crowther; Jane R Allison; Grant A Smolenski; Alison J Hodgkinson; Geoffrey B Jameson; Renwick C J Dobson
Journal:  Eur Biophys J       Date:  2018-04-16       Impact factor: 1.733

10.  Structural features of transiently modified beta-lactoglobulin relevant to the stable binding of large hydrophobic molecules.

Authors:  Evgenia Lozinsky; Stefania Iametti; Alberto Barbiroli; Gertz I Likhtenshtein; Tamás Kálai; Kálmán Hideg; Francesco Bonomi
Journal:  Protein J       Date:  2006-01       Impact factor: 4.000

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