N. A. Akhmedov, L. N. Agaeva, R. M. Abbasli, L. I. Ismailova
{"title":"Spatial Structure of the Casoxin C Molecule","authors":"N. A. Akhmedov, L. N. Agaeva, R. M. Abbasli, L. I. Ismailova","doi":"10.1134/S0006350924700052","DOIUrl":null,"url":null,"abstract":"<div><p>A theoretical conformational analysis was performed to study the conformational possibilities for the casoxin C molecule (Tyr1–Ile2–Pro3–Ile4–Gln5–Tyr6–Val7–Leu8–Ser9–Arg10–OH). The potential function of the system was chosen as a sum of non-valence, electrostatic, and torsion interactions, and the energy of hydrogen bonds. The low-energy conformations of the casoxin C molecule were found, the values of dihedral angles of the main and side chains of the amino acid residues that make up the molecule were determined, and the energy of intra- and interresidual interactions was estimated. It has been shown that the spatial structure of the casoxin C molecule is represented by conformations of eight shapes of the peptide backbone. The results obtained can be used to elucidate the structural and structural-functional organization of casoxin molecules.</p></div>","PeriodicalId":493,"journal":{"name":"Biophysics","volume":null,"pages":null},"PeriodicalIF":4.0330,"publicationDate":"2024-07-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biophysics","FirstCategoryId":"4","ListUrlMain":"https://link.springer.com/article/10.1134/S0006350924700052","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"Biochemistry, Genetics and Molecular Biology","Score":null,"Total":0}
引用次数: 0
Abstract
A theoretical conformational analysis was performed to study the conformational possibilities for the casoxin C molecule (Tyr1–Ile2–Pro3–Ile4–Gln5–Tyr6–Val7–Leu8–Ser9–Arg10–OH). The potential function of the system was chosen as a sum of non-valence, electrostatic, and torsion interactions, and the energy of hydrogen bonds. The low-energy conformations of the casoxin C molecule were found, the values of dihedral angles of the main and side chains of the amino acid residues that make up the molecule were determined, and the energy of intra- and interresidual interactions was estimated. It has been shown that the spatial structure of the casoxin C molecule is represented by conformations of eight shapes of the peptide backbone. The results obtained can be used to elucidate the structural and structural-functional organization of casoxin molecules.
为了研究 casoxin C 分子（Tyr1-Ile2-Pro3-Ile4-Gln5-Tyr6-Val7-Leu8-Ser9-Arg10-OH）的构象可能性，我们进行了理论构象分析。系统的势函数被选为非价、静电和扭转相互作用以及氢键能量的总和。找到了 Casoxin C 分子的低能构象，确定了组成分子的氨基酸残基主链和侧链的二面角值，并估算了残基内和残基间相互作用的能量。结果表明，卡索辛 C 分子的空间结构由肽骨架的八种构象表示。所获得的结果可用于阐明 casoxin 分子的结构和结构功能组织。
BiophysicsBiochemistry, Genetics and Molecular Biology-Biophysics
CiteScore
1.20
自引率
0.00%
发文量
67
期刊介绍：
Biophysics is a multidisciplinary international peer reviewed journal that covers a wide scope of problems related to the main physical mechanisms of processes taking place at different organization levels in biosystems. It includes structure and dynamics of macromolecules, cells and tissues; the influence of environment; energy transformation and transfer; thermodynamics; biological motility; population dynamics and cell differentiation modeling; biomechanics and tissue rheology; nonlinear phenomena, mathematical and cybernetics modeling of complex systems; and computational biology. The journal publishes short communications devoted and review articles.
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号
