Skip to main content
SpringerLink
Log in

Irreversible Protein Denaturation

  • Living reference work entry
  • First Online:
Encyclopedia of Biophysics

  • 2262 Accesses

Definition

Protein denaturation is said to be irreversible when the denatured state achieved by increasing temperature or by using chemical denaturants is unable to return to the native, biologically functional state upon removal of the factor that caused denaturation.

Introduction

The biological function of many proteins relies on a more or less well-defined three-dimensional structure. The process by which a linear polypeptide chain folds to a functional structure (i.e., the protein folding process) is of paramount importance in Biology and has been exhaustively studied for many years, both in vitro and in vivo. However, the processes that lead to the alteration of the native, functional structure with concomitant loss of biological function are also of great interest for a number of obvious reasons, including, for instance, that such processes may hamper industrial applications of enzymes or that they may determine the shelf life of protein pharmaceuticals.

In vitrostudies on the...

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution

Institutional subscriptions

References

  • Bohley P (1995) The fate of proteins in cells. Naturwissenschaften 82:544–550

    Article  CAS  Google Scholar 

  • Broom A, Ma SM, Xia K et al (2015) Designed protein reveals structural determinants of extreme kinetic stability. Proc Natl Acad Sci U S A 112:14605–14610

    Article  CAS  Google Scholar 

  • Godoy-Ruiz R, Ariza F, Rodriguez-Larrea D et al (2006) Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. J Mol Biol 362:966–978

    Article  CAS  Google Scholar 

  • Lim SA, Hart KM, Harms MJ, Marqusee S (2016) Evolutionary trend toward kinetic stability in the folding trajectory of RNases H. Proc Natl Acad Sci U S A 113:13045–13050

    Article  CAS  Google Scholar 

  • Lumry R, Eyring H (1954) Conformational changes in proteins. J Phys Chem 58:110–120

    Article  CAS  Google Scholar 

  • Meric G, Robinson AS, Roberts CJ (2017) Driving forces for nonnative protein aggregation and approaches to predict aggregation prone regions. Annu Rev Chem Biomol Eng 8:139–159

    Article  CAS  Google Scholar 

  • Morgan GJ, Kelly JW (2016) The kinetic stability of a full-length antibody light chain dimer determines whether endoproteolysis can release amyloidogenic variable domains. J Mol Biol 21:4280–4297

    Article  Google Scholar 

  • Plaza del Pino IM, Ibarra-Molero B, Sanchez-Ruiz JM (2000) Lower kinetic limit to protein thermal stability: a proposal regarding protein stability in vivo and its relation with misfolding diseases. Proteins 40:58–70

    Article  CAS  Google Scholar 

  • Privalov PL (1982) Stability of proteins. Proteins which do not present a single cooperative system. Adv Protein Chem 35:1–104

    Article  CAS  Google Scholar 

  • Robertson AD, Murphy KP (1997) Protein structure and the energetics of protein stability. Chem Rev 97:1251–1268

    Article  CAS  Google Scholar 

  • Sanchez-Ruiz JM (1992) Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry. Biophys J 61:921–935

    Article  CAS  Google Scholar 

  • Sanchez-Ruiz JM (2010) Protein kinetic stability. Biophys Chem 147:1–15

    Article  Google Scholar 

  • Sanchez-Ruiz JM (2016) Kinetic stability of variant enzymes. In: Svendsen A (ed) Understanding enzymes. Function, design, engineering and analysis. Pan Stanford Publishing, Singapore, pp 835–858

    Chapter  Google Scholar 

  • Toyama BH, Savas JN, Park SK et al (2013) Identification of long-lived proteins reveals exceptional stability of essential cellular structures. Cell 154:971–982

    Article  CAS  Google Scholar 

  • Xia K, Pittelli S, Church J, Colón W (2016) Kinetic stability of proteins in beans and peas: implications for protein digestibility, seed germination, and plant adaptation. J Agric Food Chem 64:7649–7657

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Departamento de Quimica Fisica, Facultad de Ciencias, Universidad de Granada, Granada, 18071, Spain

    Beatriz Ibarra-Molero & Jose M. Sanchez-Ruiz

Authors
  1. Beatriz Ibarra-Molero
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Jose M. Sanchez-Ruiz
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Jose M. Sanchez-Ruiz .

Editor information

Editors and Affiliations

  1. University Leicester MRC Centre, Leicester, United Kingdom

    Gordon Roberts

  2. Dept Biochemistry, University of Oxford, Oxford, United Kingdom

    Anthony Watts

Section Editor information

  1. School of Chemistry, University of Glasgow, Glasgow, UK

    Alan Cooper

Rights and permissions

Reprints and permissions

Copyright information

© 2018 European Biophysical Societies’ Association (EBSA)

About this entry

Check for updates. Verify currency and authenticity via CrossMark

Cite this entry

Ibarra-Molero, B., Sanchez-Ruiz, J.M. (2018). Irreversible Protein Denaturation. In: Roberts, G., Watts, A. (eds) Encyclopedia of Biophysics. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-35943-9_10067-1

Download citation

  • DOI: https://doi.org/10.1007/978-3-642-35943-9_10067-1

  • Received:

  • Accepted:

  • Published:

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-35943-9

  • Online ISBN: 978-3-642-35943-9

  • eBook Packages: Springer Reference Biomedicine and Life SciencesReference Module Biomedical and Life Sciences

Publish with us

Policies and ethics

Search

Navigation