Conformational aspects in the formation of structures of the backbone of polypeptide chains in proteins. Relationship between conformational stability/lability and β-turns

Yu. Yu Torshin; Торшин И. Ю; I. V Filatov; Филатов И. В; A. V Batyanovskii; Батяновский А. В; K. V Smirnov; Смирнов К. В; A. A Anashkina; Анашкина А. А; N. G Esipova; Есипова Н. Г; V. G Tumanyan; Туманян В. Г

doi:10.31857/S0006302923010015

Conformational aspects in the formation of structures of the backbone of polypeptide chains in proteins. Relationship between conformational stability/lability and β-turns

Авторлар: Torshin Y.¹, Filatov I.², Batyanovskii A.³, Smirnov K.⁴, Anashkina A.⁴, Esipova N.⁴, Tumanyan V.⁴
Мекемелер:
1. Dorodnicyn Computing Centre, Russian Academy of Sciences
2. Moscow Institute of Physics and Technology
3. Institute of Biophysics and Cell Engineering, National Academy of Sciences of Belarus
4. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences
Шығарылым: Том 68, № 1 (2023)
Беттер: 5-10
Бөлім: Articles
URL: https://journals.rcsi.science/0006-3029/article/view/144399
DOI: https://doi.org/10.31857/S0006302923010015
EDN: https://elibrary.ru/NYMYUD
ID: 144399

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Аннотация

To assess the nature of the relationship between the integral conformational stability of tetrapeptides and the main types of β-turns (which are also tetrapeptides), calculations were performed using spectrum diagrams and asymmetry in the distribution of conformationally stable and unstable tetrapeptides. It was shown that type I', II, and II' β-turns are comprised of predominantly conformationally labile peptides, that is consistent with the predetermined nature of their structure as described earlier. As previously shown in our study, in this case the conformation is imposed by external conditions (namely the cycle closuring) and the prevalence of conformationally labile peptides facilitates the formation of the structure by virtue of external factors. Type I β-turn is an exception: peptides with different conformational lability are fairly evenly distributed. Most likely, this indicates that the formation of the type I β-turn is not predetermined.

Негізгі сөздер

conformational stable/labile segments of protein, Local protein structure, conformational analysis, β-turns, statistical analysis, molecular dynamics

Әдебиет тізімі

W. Kabsch and C. Sander, Biopolymers, 22 (12), 2577 (1983).
X. de la Cruz, E. G. Hutchinson, A. Shepherd, and J. M. Thornton, Proc. Natl. Acad. Sci. USA, 99 (17), 11157 (2002).
M. Kumar, M. Bhasin, N. K. Natt, and G. P. S. Raghava, Nucl. Acids Res., 33, W154 (2005).
M. K. Elbashir, J. Wang, F. X. Wu, et al., Proteome Sci., 11 (Suppl. 1), S5 (2013).
C. Fang, Y. Shang, and D. Xu, Proteins, 88 (1), 143 (2020).
A. G. de Brevern, Sci. Reports, 6, 33191 (2016).
Л. А. Уpошлев, И. Ю. Тоpшин, А. В. Батяновcкий и др., Биофизика, 60 (1), 5 (2015).
Л. А. Уpошлев, И. Ю. Тоpшин, А. В. Батяновcкий и др., Биофизика, 64 (2), 272 (2019).
И. Ю. Тоpшин, А. В. Батяновcкий, Л. А. Уpошлев и др., Биофизика, 64 (2), 256 (2019).
Ю. И. Журавлёв, К. В. Рудаков и И. Ю. Торшин, Труды МФТИ, 3 (4), 45 (2011).

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Conformational aspects in the formation of structures of the backbone of polypeptide chains in proteins. Relationship between conformational stability/lability and β-turns

Толық мәтін

Аннотация

Негізгі сөздер

Авторлар туралы

Yu. Torshin

I. Filatov

A. Batyanovskii

K. Smirnov

A. Anashkina

N. Esipova

V. Tumanyan

Әдебиет тізімі

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