English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

The folding of a peptide chain into a three dimensional structure is athermodynamically driven process such that the chain naturally evolves to formdomains of similar amino acids. The formation of this domain occurs by curlingthe one dimensional amino acid sequence by moving similar amino acids proximityto each other. We model this formation of domains or ordering of amino acidsusing q-state Potts model and study the thermodynamic properties using astatistical mechanics approach. Converting the interacting amino acids into aneffectively non-interacting model using a mean-field theory, we calculate theHelmholtz free energy (HFE). Then by investigating the HFE, we study theproperties of protein folding transition qualitatively. We find that theprotein folding phase transition is a strongly first order and the specificheat shows the experimental signatures of this phase transition. Further, wecompare these mean-field results with exact transfer matrix results in onedimension and then large $q$ expansion results in two dimensions.

A statistical mechanics perspective for protein folding from $q$-state Potts model