Repozitorij Univerze v Novi Gorici

Izpis gradiva
A+ | A- | Pomoč | SLO | ENG

Naslov:Spin Model of Protein Conformations in water: Theory vs Experiment.
Avtorji:ID Badasyan, Artem, UNG (Avtor)
ID Yeritsyan, Knarik (Avtor), et al.
Datoteke: Gradivo nima datotek, ki so prostodostopne za javnost. Gradivo je morda fizično dosegljivo v knjižnici fakultete, zalogo lahko preverite v COBISS-u. Povezava se odpre v novem oknu
Jezik:Angleški jezik
Vrsta gradiva:Delo ni kategorizirano
Tipologija:1.10 - Objavljeni povzetek znanstvenega prispevka na konferenci (vabljeno predavanje)
Organizacija:UNG - Univerza v Novi Gorici
Opis:Background (approx. 70 words) I will overview the application of spin models of Statistical Mechanics to describe polypeptide conformations. Zimm and Bragg model is one of the most successful examples of such approach [1]. In 2010 we have suggested the microscopic formulation of the model [2], which was later augmented by including the interactions with water [3]. Adding the solvent opened doors for the direct comparisons with UV-vis, Circular Dichroism (CD) and Differential Scanning Calorimetry (DSC) experiments. Aim (approx. 30 words) Based on a statistical Potts-like spin model of protein folding we provide formulas for experimentally measurable quantities and report a perfect fit. Our approach suggest a new method to process the results of protein folding experiments. Method (approx. 100 words) We start from the microscopic Hamiltonian formulation of the polypeptide model in water and use the usual Statistical Mechanics route from the model to partition function and the thermodynamics. Using Mayer expansion and summation over the solvent degrees of freedom, the problem is shown to be equivalent to in vacuo model with some effective, temperature dependent interaction energy. Estimated partition function leads to the expressions for the thermodynamic potentials and order parameter averages. The comparison (least-square fit) with the experimental data points from CD and DSC experiments on protein folding allows to extract the information on hydrogen bonding strengths, not available with the classical approach. Results & Discussion (approx 200 words, or less if you paste an image or insert a table ) Proposed model allows for the cold denaturation under certain well-defined conditions. The agreement between the theoretical curves and data points is excellent, and the values of fitted parameters are within the expected ranges. The limitations of the approach are naturally related to the limitations of the Zimm-Bragg original model, intended to describe the changes of the secondary structure elements only. Taking into account that the so-called “two-state” model widely used nowadays to process the experiment does not contain any info regarding the hydrogen bonding energies, the method we suggest provides a promising alternative. Conclusion (70 words approximately) The proposed approach does what it is intended to do: processing of the experimental data on protein folding. However the model contains the very same serious limitations, as the two-state model: it is oversimplified in many respects. Whether the currently available experimental methods need a better model than already suggested ones or not, is an open question. References: [1] Zimm, B.H.; Bragg, J.K.; J. Chem. Phys. 31:526–535 (1959). [2] Badasyan, A.V. et al., Phys. Rev. E 81:021921 (2010). [3] Badasyan, A.V. et al., Phys. Rev. E 89:022723 (2014). [4] Badasyan, A. et al.; Eur.Phys. J. E 36:1–9 (2013).
Ključne besede:Protein folding, CD, DSC, Zimm-Bragg
Status publikacije:Posredovano založniku
Št. strani:2 str
PID:20.500.12556/RUNG-8202 Novo okno
COBISS.SI-ID:152137731 Novo okno
Datum objave v RUNG:15.05.2023
Število ogledov:1660
Število prenosov:0
Kopiraj citat
Skupna ocena:(0 glasov)
Vaša ocena:Ocenjevanje je dovoljeno samo prijavljenim uporabnikom.
Objavi na:Bookmark and Share

Postavite miškin kazalec na naslov za izpis povzetka. Klik na naslov izpiše podrobnosti ali sproži prenos.

Gradivo je del monografije

Naslov:International Conference on Materials & Processes for Sustainable Development 2023 : May 10 & 11, 2023, Chenini, Gabes - Tunisia
Kraj izida:[Tunisia
Založnik:s. n.]
Leto izida:2023
COBISS.SI-ID:152136707 Novo okno