Pregled bibliografske jedinice broj: 1216622
New structural features that significantly improve protein folding rate models
New structural features that significantly improve protein folding rate models // 3rd International PhysicsConference in Bosnia and Herzegovina : Book of Abstracts / Milošević, Dejan ; Habibović, Dino (ur.).
Sarajevo: Physical Society in Federation of Bosnia and Herzegovina, 2022. str. 18-18 (pozvano predavanje, recenziran, sažetak, znanstveni)
CROSBI ID: 1216622 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
New structural features that significantly improve protein folding rate models
Autori
Lučić, Bono ; Kraljević, Antonija ; Batista, Jadranko
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
3rd International PhysicsConference in Bosnia and Herzegovina : Book of Abstracts
/ Milošević, Dejan ; Habibović, Dino - Sarajevo : Physical Society in Federation of Bosnia and Herzegovina, 2022, 18-18
Skup
3rd International Physics Conference in Bosnia and Herzegovina (PHYCONBA 2022)
Mjesto i datum
Sarajevo, Bosna i Hercegovina, 30.06.2022. - 01.07.2022
Vrsta sudjelovanja
Pozvano predavanje
Vrsta recenzije
Recenziran
Ključne riječi
protein folding rates ; prediction ; sequence-based attributes, secondary structure segments ; secondary structure entropy ; distance
Sažetak
The study of protein folding is attractive to scientists from various natural sciences, including physicists/biophysicists [1]. One of them is M. Karplus, Nobel laureate 2013, who modelled protein folding and unfolding of 33 proteins using models selected from 24 generated sequence-based features/descriptors [2]. Protein folding rates correlate with protein length (the total number of amino acids in a protein), the content of secondary structures in the protein, the absolute and relative mean distance of contact order between amino acids, etc. [3]. We have defined and introduced several new sequence-based attributes/features suitable for modelling the folding rates of proteins, such as the features related to the secondary structure of proteins (segments of alpha or beta secondary structure) and the average distance of amino acids. Models were also developed with different combinations of the above features. Improved models have been developed to predict the folding rates of proteins and all features are not dependent on the 3D structure of the protein. References: [1] D.N. Ivankov, A.V. Finkelstein, Biomolecules 10, 250 (2020) [2] A. R. Dinner, S. S. So, M. Karplus, Advan. Chem. Phys. 120, 1 (2002) [3] H. Zhou, Y. Zhou, Biophys. J. 82, 458 (2002)
Izvorni jezik
Engleski
Znanstvena područja
Fizika, Kemija, Interdisciplinarne prirodne znanosti
Napomena
Basic grant of MZO/RBI to Bono Lučić
Participant-lecturer: Bono Lučić
POVEZANOST RADA
Projekti:
EK-KF-KK.01.1.1.01.0002 - Bioprospecting Jadranskog mora (Jerković, Igor; Dragović-Uzelac, Verica; Šantek, Božidar; Čož-Rakovac, Rozelinda; Kraljević Pavelić, Sandra; Jokić, Stela, EK ) ( CroRIS)
Ustanove:
Institut "Ruđer Bošković", Zagreb
Profili:
Bono Lučić
(autor)