Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Protein folding as a nonlinear nonequilibrium thermodynamic process.

E M Popov1

  • 1Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.

Biochemistry and Molecular Biology International
|April 16, 1999
PubMed
Summary

A new bio-bifurcation theory explains protein folding as a series of specific, non-equilibrium fluctuations. This model accounts for the stochastic nature, speed, and precision of protein self-assembly, highlighting entropy's constructive role.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

[Mechanism of aspartyl proteinase action. VII. Noncovalent complexes of HIV-1 aspartyl proteinase with substrate and substrate-like inhibitors].

Bioorganicheskaia khimiia·2000
Same author

[Mechanism of action of aspartyl proteinases. VI. Nonvalent enzyme-inhibitory and enzyme-substrate complexes of the aspartyl proteinase rhizopus pepsin].

Bioorganicheskaia khimiia·2000
Same author

[Mechanism of action of aspartic proteinases. V. Conformational characteristics of fragments of substrate-binding sites in rhizopuspepsin and HIV-1 proteinase].

Bioorganicheskaia khimiia·1999
Same author

Mechanism of action of aspartic proteases.

Advances in experimental medicine and biology·1998
Same author

Theory and method of a priori computation of catalytic acts of aspartic and serine proteinases.

Advances in experimental medicine and biology·1998
Same author

[Mechanism of action of aspartic proteinases. 2. Conformational possibilities of an HIV-1 proteinase substrate].

Bioorganicheskaia khimiia·1996

Area of Science:

  • Biophysics
  • Computational Biology
  • Protein Science

Background:

  • Protein folding is crucial for biological function.
  • Existing models struggle to explain the speed and precision of protein self-assembly.
  • The role of entropy in forming ordered protein structures from disordered states requires further clarification.

Purpose of the Study:

  • To develop a novel bio-bifurcation theory for protein folding.
  • To explain key characteristics of protein folding, including stochasticity, speed, and precision.
  • To elucidate the constructive role of entropy in protein structure formation.

Main Methods:

  • Development of the bio-bifurcation theory.
  • Analysis of protein folding as a sequence of non-equilibrium irreversible fluctuations.

Related Experiment Videos

  • Numerical methods for a priori calculation of polypeptide structures based on the bifractional folding model.

    • Main Results:

    • The bio-bifurcation model successfully explains the stochastic mechanism, short folding times, and high precision of protein self-assembly.
    • The theory provides a framework for understanding how entropy contributes constructively to forming highly ordered protein structures.
    • A numerical method for predicting polypeptide structures using the bifractional folding model is presented.

    Conclusions:

    • The bio-bifurcation theory offers a comprehensive explanation for protein folding dynamics.
    • This model advances our understanding of protein self-assembly and the role of entropy.
    • The presented numerical method enables a priori structure calculations, aiding in protein design and research.