Hdl Handle:
http://hdl.handle.net/10675.2/621319
Title:
Thermodynamic Properties of Protein Folding Process
Authors:
Sivised, Vattika; De Silva, Theja
Abstract:
Proteins are one of the fundamental building blocks of life and they are present in almost all biological and cellular processes. Proteins consist of amino acids held together in a long chain by peptide bonds. When proteins function in biological processes, they fold in to three-dimensional structures by curling the chain. The folding of a peptide chain into a three dimensional structure is a thermodynamically driven process such that the chain naturally evolves to form domains of similar amino acids. The formation of this domain occurs by curling the one dimensional amino acid sequence by moving similar amino acids proximity to each other. We model this formation of domains or “ordering of amino acids” using q-state Potts model and study the thermodynamic Properties using a statistical mechanics approach. Converting the interacting amino acids into an effectively non-interacting model using a mean-field theory, we calculate the Helmholtz free energy (HFE). Then by investigating the HFE, we qualitatively study the properties of protein folding transition. We find that the protein folding phase transition is strongly first order and the specific heat shows the experimental signatures of this phase transition.
Affiliation:
Department of Chemistry & Physics
Issue Date:
Mar-2017
URI:
http://hdl.handle.net/10675.2/621319
Type:
Presentation
Language:
en
Description:
Presentation given at the 18th Annual Phi Kappa Phi Student Research and Fine Arts Conference
Appears in Collections:
Department of Chemistry and Physics: Student Research and Presentations; 18th Annual PKP Student Research and Fine Arts Conference: Oral Symposia IV

Full metadata record

DC FieldValue Language
dc.contributor.authorSivised, Vattikaen
dc.contributor.authorDe Silva, Thejaen
dc.date.accessioned2017-03-06T20:49:33Z-
dc.date.available2017-03-06T20:49:33Z-
dc.date.issued2017-03-
dc.identifier.urihttp://hdl.handle.net/10675.2/621319-
dc.descriptionPresentation given at the 18th Annual Phi Kappa Phi Student Research and Fine Arts Conferenceen
dc.description.abstractProteins are one of the fundamental building blocks of life and they are present in almost all biological and cellular processes. Proteins consist of amino acids held together in a long chain by peptide bonds. When proteins function in biological processes, they fold in to three-dimensional structures by curling the chain. The folding of a peptide chain into a three dimensional structure is a thermodynamically driven process such that the chain naturally evolves to form domains of similar amino acids. The formation of this domain occurs by curling the one dimensional amino acid sequence by moving similar amino acids proximity to each other. We model this formation of domains or “ordering of amino acids” using q-state Potts model and study the thermodynamic Properties using a statistical mechanics approach. Converting the interacting amino acids into an effectively non-interacting model using a mean-field theory, we calculate the Helmholtz free energy (HFE). Then by investigating the HFE, we qualitatively study the properties of protein folding transition. We find that the protein folding phase transition is strongly first order and the specific heat shows the experimental signatures of this phase transition.en
dc.language.isoenen
dc.subjectProtein Foldingen
dc.subjectMean-Field Theoryen
dc.subjectAmino Acids Sequenceen
dc.titleThermodynamic Properties of Protein Folding Processen
dc.typePresentationen
dc.contributor.departmentDepartment of Chemistry & Physicsen
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