Literature DB >> 10424909

Modeling of irreversible thermal protein denaturation at varying temperature. II. The complete kinetic model of Lumry and Eyring.

A E Lyubarev1, B I Kurganov.   

Abstract

The model for thermal denaturation of proteins involving consecutive reversible and irreversible steps (Lumry and Eyring model) has been analyzed. The most general case, when equilibrium in the first step is established slowly in comparison with the rate of the second step and the heat effect value for the second step is either greater than or less than zero, has been considered. The theoretical dependences of excess heat capacity on temperature have been constructed. The variation of the shape of the theoretical curves with varied values of the enthalpy change for the second step, Arrhenius equation parameters for both steps, and the scanning rate has been studied.

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Year:  1999        PMID: 10424909

Source DB:  PubMed          Journal:  Biochemistry (Mosc)        ISSN: 0006-2979            Impact factor:   2.487


  3 in total

1.  Exploration of Protein Unfolding by Modelling Calorimetry Data from Reheating.

Authors:  Stanislav Mazurenko; Antonin Kunka; Koen Beerens; Christopher M Johnson; Jiri Damborsky; Zbynek Prokop
Journal:  Sci Rep       Date:  2017-11-24       Impact factor: 4.379

Review 2.  A Conceptual Framework for Integrating Cellular Protein Folding, Misfolding and Aggregation.

Authors:  Seong Il Choi; Baik L Seong
Journal:  Life (Basel)       Date:  2021-06-24

3.  Multi-state proteins: approach allowing experimental determination of the formation order of structure elements in the green fluorescent protein.

Authors:  Tatiana N Melnik; Tatiana V Povarnitsyna; Anatoly S Glukhov; Bogdan S Melnik
Journal:  PLoS One       Date:  2012-11-14       Impact factor: 3.240

  3 in total

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