Department of Chemical and Biological Engineering2024-11-0920129789-8984-2590-410.5220/00037852022002252-s2.0-84861996003http://dx.doi.org/10.5220/0003785202200225https://hdl.handle.net/20.500.14288/8749Denatured 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.EngineeringChemical biological engineeringConference proceedinghttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84861996003andpartnerID=40andmd5=ceb7162ce52964a3acdc7686b05a8481310729400029N/A2735