Statistical mechanics of proteins in the random coil state

Cigdem Sevim Bayrak, Burak Erman

Research output: Chapter in Book/Report/Conference proceedingConference contributionpeer-review

Abstract

Denatured proteins are mostly partially folded and compact proteins. A statistical analysis on thermodynamic properties is presented to describe and characterize denatured proteins. Conformational free energy, energy, entropy and heat capacity expressions are derived using the Rotational Isomeric States model of polymer theory. The state space and the probabilities of each state are comprised from a coil database. Properties for the denatured state are obtained for a sample set of proteins taken from the Protein Data Bank. Thermodynamic expressions of denatured state are derived.

Original languageEnglish
Title of host publicationBIOINFORMATICS 2012 - Proceedings of the International Conference on Bioinformatics Models, Methods and Algorithms
Pages220-225
Number of pages6
StatePublished - 2012
Externally publishedYes
EventInternational Conference on Bioinformatics Models, Methods and Algorithms, BIOINFORMATICS 2012 - Vilamoura, Algarve, Portugal
Duration: 1 Feb 20124 Feb 2012

Publication series

NameBIOINFORMATICS 2012 - Proceedings of the International Conference on Bioinformatics Models, Methods and Algorithms

Conference

ConferenceInternational Conference on Bioinformatics Models, Methods and Algorithms, BIOINFORMATICS 2012
Country/TerritoryPortugal
CityVilamoura, Algarve
Period1/02/124/02/12

Keywords

  • Denatured state
  • Random coil
  • Rotational isomeric state

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