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Naslov:Differential scanning calorimetry of proteins and Zimm–Bragg model in water
Avtorji:ID Yeritsyan, Knarik (Avtor)
ID Badasyan, Artem (Avtor)
Datoteke:URL https://www.sciencedirect.com/science/article/pii/S0003986124002546
 
.pdf 1-s2.0-S0003986124002546-main.pdf (645,94 KB)
MD5: 4EB1C30037AD50AFB66D2BEE04038E71
 
Jezik:Angleški jezik
Vrsta gradiva:Neznano
Tipologija:1.01 - Izvirni znanstveni članek
Organizacija:UNG - Univerza v Novi Gorici
Opis: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.
Ključne besede:protein folding, differential scanning calorimetry, heat capacity, two-state model, Hawley model
Status publikacije:Objavljeno
Verzija publikacije:Objavljena publikacija
Datum objave:01.10.2024
Leto izida:2019
Št. strani:str. 1-6
Številčenje:Vol. 760, [article no.] ǂ110132
PID:20.500.12556/RUNG-9235 Novo okno
ISSN:0003-9861
COBISS.SI-ID:205311491 Novo okno
UDK:53
ISSN pri članku:0003-9861
DOI:10.1016/j.abb.2024.110132 Novo okno
NUK URN:URN:SI:UNG:REP:K5BPRYA9
Datum objave v RUNG:26.08.2024
Število ogledov:290
Število prenosov:2
Metapodatki:XML RDF-CHPDL DC-XML DC-RDF
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Vaša ocena:Ocenjevanje je dovoljeno samo prijavljenim uporabnikom.
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Gradivo je del revije

Naslov:Archives of biochemistry and biophysics
Skrajšan naslov:Arch. biochem. biophys.
Založnik:Academic Press.
ISSN:0003-9861
COBISS.SI-ID:3219471 Novo okno

Gradivo je financirano iz projekta

Financer:ARIS - Javna agencija za znanstvenoraziskovalno in inovacijsko dejavnost Republike Slovenije
Številka projekta:P2-0412
Naslov:Heterogeni procesi na površinah trdnin za trajnostne tehnologije

Licence

Licenca:CC BY-NC 4.0, Creative Commons Priznanje avtorstva-Nekomercialno 4.0 Mednarodna
Povezava:http://creativecommons.org/licenses/by-nc/4.0/deed.sl
Opis:Licenca Creative Commons, ki prepoveduje komercialno uporabo, vendar uporabniki ne rabijo upravljati materialnih avtorskih pravic na izpeljanih delih z enako licenco.
Začetek licenciranja:20.08.2024

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