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Title:Water reveals non-Arrhenius kinetics in protein folding experiments
Authors:Badasyan, Artem (Authorship owner)
Badasyan, Artem (Author)
Files:.pdf Abstract-Book_IOCFN_July2020.pdf (2,35 MB)
 
Language:English
Work type:Not categorized (r6)
Tipology:1.10 - Published Scientific Conference Contribution Abstract (invited lecture)
Organization:UNG - University of Nova Gorica
Abstract:Statistical theories describe systems in equilibrium, and cannot be used to study kinetics. However, the theo- ries are based on coarse-grained parameters, that include assumptions regarding the underlying kinetics. If such assumptions are incorrect, the theoretical expressions, used to process the experimental data, will not fit. I report on one such case we have met within the application of Zimm-Bragg [1] theory to process folding experiments, and discuss the reasons and consequences. Studies of relaxation phenomena in glass-forming liquids by default account for the shift in temperature by some value, corresponding to the glass formation temperature, .In particular, temperature shift appears in hydrated proteins because of the presence of partially glassy states giving rise to non- Arrhenius relaxation times log τ ~ [2]. A phenomenological approach was suggested by Adam and Gibbs as early as in 1965 to describe the sudden increase of viscosity and the slowing down of the collective modes in super-cooled liquids as the temperature is approaching[3]. The key idea of Adam-Gibbs theory was to consider the supercooled liquid as a set of clusters (cooperatively rearranging regions) of different sizes that change with temperature, giving rise to the shift in re- laxation time. The temperature shift factor is present in many theories describing properties of water. Thus, Truskett and Dill had to include the Adamm-Gibbs temperature shift into their simple analytical model of water to achieve the agreement with experimental data on the tem- perature dependence of self-diffusion coefficient [4]. Later, Schiro and Weik have summarised recent in vitro and in silico experimental results regarding the role of hydration water in the onset of protein structural dy- namics, and have reported the presence of super-Arrhenius relaxation region above the ”protein dynamic transition” temperature [4]. Recently, Mallamace et al have used the Adam-Gibbs theory in their NMR meas- urements of protein folding-unfolding in water [4] and to rationalise the complicated pressure-temperature diagrams in these glass-forming systems. Motivated by the considerations above, and taking into account the relationship between the unimolecular rate of folding in water and the relaxation time 45 , we introduce the tem- perature shift into the formulas used to fit experimental data on hydrated polypeptides. By doing so we resolve the paradox and complete the new method of processing the Circular Dichroism ex- perimental data on protein folding
Keywords:water, protein folding, non-Arrhenius kinetics
Year of publishing:2020
Number of pages:1
COBISS_ID:23055107 Link is opened in a new window
URN:URN:SI:UNG:REP:RVBL17HE
Views:963
Downloads:49
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Record is a part of a monograph

Title:International Online Conference on Functional Nanomaterials, 15-16 July 2020, Abstract Book
Conference organizer:European Nanoscience and Nanotechnology Association
Collection numbering:010
Collection ISSN:2683-1031
Place of publishing:Sofia, Bulgaria
Year of publishing:2020

Document is financed by a project

Funder:ARRS - Agencija za raziskovalno dejavnost Republike Slovenije (ARRS)
Funding Programme:Raziskovalni projekti - temeljni
Project no.:J1-1705
Name:
Acronym:
Project ID:info:eu-repo/grantAgreement/ARRS/Raziskovalni%20projekti%20-%20temeljni/J1-1705

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