Naslov: | Modelling water for calorimetry of proteins |
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Avtorji: | ID Yeritsyan, Knarik (Avtor) ID Badasyan, Artem (Avtor) |
Datoteke: |
Gradivo nima datotek, ki so prostodostopne za javnost. Gradivo je morda fizično dosegljivo v knjižnici fakultete, zalogo lahko preverite v COBISS-u. |
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Jezik: | Angleški jezik |
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Vrsta gradiva: | Neznano |
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Tipologija: | 1.12 - Objavljeni povzetek znanstvenega prispevka na konferenci |
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Organizacija: | UNG - Univerza v Novi Gorici
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Opis: | Differential Scanning Calorimetry (DSC) is a powerful technique used to study the thermal stability and unfolding of proteins. DSC provides the excess heat capacity profile and is used to study the thermodynamics of a given protein. By fitting DSC data to the model, researchers can obtain valuable information about the thermodynamics of protein folding and unfolding, which can help them better understand protein structure, stability, and function.
Based on Hamiltonian representation of ZB model and using the solvent effects we derived an expression for heat capacity in proteins and successfuly fit it to experimental data. As we show, our model provides a better fit to experimental data, as compared to the 2-state model. The model we propose takes into account also water effects and we show that it fits better to experimental data giving inter- and intra-molecular H-bonding energies instead of reporting only one total enthalpy. |
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Ključne besede: | Zimm-Bragg model, water model, helix-coil transition, protein folding, differential scanning calorimetry |
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Leto izida: | 2023 |
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Št. strani: | 1 str. |
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PID: | 20.500.12556/RUNG-8590-44dfa3e7-ffa0-41d9-06b4-ab76de11c509 |
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COBISS.SI-ID: | 168900867 |
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UDK: | 54 |
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NUK URN: | URN:SI:UNG:REP:DPPPESI8 |
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Datum objave v RUNG: | 18.10.2023 |
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Število ogledov: | 1958 |
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Število prenosov: | 0 |
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