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dc.contributor.authorLazaridis, T.en
dc.contributor.authorArchontis, Georgios Z.en
dc.contributor.authorKarplus, M.en
dc.creatorLazaridis, T.en
dc.creatorArchontis, Georgios Z.en
dc.creatorKarplus, M.en
dc.date.accessioned2019-12-02T15:31:40Z
dc.date.available2019-12-02T15:31:40Z
dc.date.issued1995
dc.identifier.urihttp://gnosis.library.ucy.ac.cy/handle/7/58815
dc.description.abstractThis chapter discusses published analyses of protein stability based on model compound data and outlines the assumptions that have been made. The enthalpy of protein folding is considered and a thermodynamic cycle is used to relate the measurements to quantities that can be calculated. The focus is on the enthalpy of denaturation because it is most directly accessible to calculations. The experiments and analysis of Privalov and co-workers, particularly which of Makhatadze and Privalov are considered in detail because these measurements provide the most complete results on the thermodynamics of proteins. The estimates of internal van der Waals and hydrogen bonding contributions to the enthalpy difference between the native and denatured states of the protein are compared with the calculations of the van der Waals and electrostatic terms (the latter includes hydrogen bonding) from an atom-based model. Statistical mechanical calculations and molecular dynamics simulations are used to estimate the difference in solvation enthalpy, as well as the free energy, of the native and unfolded states. © 1995, Academic Press Inc.en
dc.sourceAdvances in Protein Chemistryen
dc.source.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-0029094346&doi=10.1016%2fS0065-3233%2808%2960547-1&partnerID=40&md5=d77ca58cd079825ca16e5327c4176d15
dc.subjectdecompositionen
dc.subjectpriority journalen
dc.subjectreviewen
dc.subjectPeptidesen
dc.subjectentropyen
dc.subjectthermodynamicsen
dc.subjecthydrogen bonden
dc.subjectprotein foldingen
dc.subjectmolecular dynamicsen
dc.subjectprotein protein interactionen
dc.subjectProteinsen
dc.subjectProtein Conformationen
dc.subjectprotein stabilityen
dc.subjectSupport, U.S. Gov't, P.H.S.en
dc.subjectSupport, U.S. Gov't, Non-P.H.S.en
dc.subjectModels, Molecularen
dc.subjectSolventsen
dc.subjectenthalpyen
dc.subjectHydrogen Bondingen
dc.subjectprotein denaturationen
dc.titleEnthalpic Contribution to Protein Stability: Insights from Atom-Based Calculations and Statistical Mechanicsen
dc.typeinfo:eu-repo/semantics/article
dc.identifier.doi10.1016/S0065-3233(08)60547-1
dc.description.volume47
dc.description.issueCen
dc.description.startingpage231
dc.description.endingpage306
dc.author.facultyΣχολή Θετικών και Εφαρμοσμένων Επιστημών / Faculty of Pure and Applied Sciences
dc.author.departmentΤμήμα Φυσικής / Department of Physics
dc.type.uhtypeArticleen
dc.description.notes<p>Cited By :154</p>en
dc.source.abbreviationAdv. Protein Chem.en
dc.contributor.orcidArchontis, Georgios Z. [0000-0002-7750-8641]
dc.gnosis.orcid0000-0002-7750-8641


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