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Title:Differential scanning calorimetry of proteins and Zimm–Bragg model in water
Authors:ID Yeritsyan, Knarik (Author)
ID Badasyan, Artem (Author)
Files:URL https://www.sciencedirect.com/science/article/pii/S0003986124002546
 
.pdf 1-s2.0-S0003986124002546-main.pdf (645,94 KB)
MD5: 4EB1C30037AD50AFB66D2BEE04038E71
 
Language:English
Work type:Unknown
Typology:1.01 - Original Scientific Article
Organization:UNG - University of Nova Gorica
Abstract:Differential Scanning Calorimetry (DSC) is a regular and powerful tool to measure the specific heat profile of various materials. Hydrogen bonds play a crucial role in stabilizing the three-dimensional structure of proteins. Naturally, information about the strength of hydrogen bonds is contained in the measured DSC profiles. Despite its obvious importance, there is no approach that would allow the extraction of such information from the heat capacity measurements. In order to connect the measured profile to microscopic properties of a polypeptide chain, a proper model is required to fit. Using recent advances in the Zimm–Bragg (ZB) theory of protein folding in water, we propose a new and efficient algorithm to process the DSC experimental data and to extract the H-bonding energy among other relevant constants. Thus, for the randomly picked set of 33 proteins, we have found a quite narrow distribution of hydrogen bonding energies from 1 to 8 kJ/mol with the average energy of intra-protein hydrogen bonds kJ/mol and the average energy of water–protein bonds as kJ/mol. This is an important illustration of a tiny disbalance between the water–protein and intraprotein hydrogen bonds. Fitted values of the nucleation parameter belong to the range from 0.001 to 0.01, as expected. The reported method can be considered as complementary to the classical two-state approach and together with other parameters provides the protein–water and intraprotein H-bonding energies, not accessible within the two-state paradigm.
Keywords:protein folding, differential scanning calorimetry, heat capacity, two-state model, Hawley model
Publication status:Published
Publication version:Version of Record
Publication date:01.10.2024
Year of publishing:2019
Number of pages:str. 1-6
Numbering:Vol. 760, [article no.] ǂ110132
PID:20.500.12556/RUNG-9235 New window
COBISS.SI-ID:205311491 New window
ISSN:0003-9861
UDC:53
ISSN on article:0003-9861
DOI:10.1016/j.abb.2024.110132 New window
NUK URN:URN:SI:UNG:REP:K5BPRYA9
Publication date in RUNG:26.08.2024
Views:289
Downloads:2
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Record is a part of a journal

Title:Archives of biochemistry and biophysics
Shortened title:Arch. biochem. biophys.
Publisher:Academic Press.
ISSN:0003-9861
COBISS.SI-ID:3219471 New window

Document is financed by a project

Funder:ARIS - Slovenian Research and Innovation Agency
Project number:P2-0412
Name:Heterogeni procesi na površinah trdnin za trajnostne tehnologije

Licences

License:CC BY-NC 4.0, Creative Commons Attribution-NonCommercial 4.0 International
Link:http://creativecommons.org/licenses/by-nc/4.0/
Description:A creative commons license that bans commercial use, but the users don’t have to license their derivative works on the same terms.
Licensing start date:20.08.2024

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