{"title":"ob -折叠Π-modules氨基酸序列的结构与特征","authors":"E. Brazhnikov, A. V. Efimov","doi":"10.17537/2022.17.441","DOIUrl":null,"url":null,"abstract":"\n Stereochemical analysis has been performed for П-modules from the large set of non-homologous protein structures containing the OB-fold. That module consists of two β-strands connected by a loop and placed in different sheets in such a way which looks as Greek letter П. Total 70 non-homologous proteins at resolution not less than 2.5Å have been selected for the analysis from 265 suitable structures belonging to sixteen OB-fold super families. We have disclosed two types of П-modules: the fist with the connecting loop containing α-helix, and second one without helix. Entrance of protein chain into second β-sheet is carried out by the same arch with conformation βββαLβp. In most cases, 85 % of total, α-positions are occupied by glycine residue, while at entrance in the loop such residues are absent. Occupancy frequency of П-modules has been obtained in dependence on the loop length. Spatial pathway of structures of all modules are superimposed very well. Structural alignment of amino acid for П-module sequences allows us to determine the key positions of the hydrophobic, hydrophilic, and glycine residues. \n","PeriodicalId":53525,"journal":{"name":"Mathematical Biology and Bioinformatics","volume":"192 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2022-12-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Structure and features of amino acid sequences of Π-modules in OB-folds\",\"authors\":\"E. Brazhnikov, A. V. Efimov\",\"doi\":\"10.17537/2022.17.441\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"\\n Stereochemical analysis has been performed for П-modules from the large set of non-homologous protein structures containing the OB-fold. That module consists of two β-strands connected by a loop and placed in different sheets in such a way which looks as Greek letter П. Total 70 non-homologous proteins at resolution not less than 2.5Å have been selected for the analysis from 265 suitable structures belonging to sixteen OB-fold super families. We have disclosed two types of П-modules: the fist with the connecting loop containing α-helix, and second one without helix. Entrance of protein chain into second β-sheet is carried out by the same arch with conformation βββαLβp. In most cases, 85 % of total, α-positions are occupied by glycine residue, while at entrance in the loop such residues are absent. Occupancy frequency of П-modules has been obtained in dependence on the loop length. Spatial pathway of structures of all modules are superimposed very well. Structural alignment of amino acid for П-module sequences allows us to determine the key positions of the hydrophobic, hydrophilic, and glycine residues. \\n\",\"PeriodicalId\":53525,\"journal\":{\"name\":\"Mathematical Biology and Bioinformatics\",\"volume\":\"192 1\",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2022-12-06\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Mathematical Biology and Bioinformatics\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.17537/2022.17.441\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"Mathematics\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Mathematical Biology and Bioinformatics","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.17537/2022.17.441","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"Mathematics","Score":null,"Total":0}
Structure and features of amino acid sequences of Π-modules in OB-folds
Stereochemical analysis has been performed for П-modules from the large set of non-homologous protein structures containing the OB-fold. That module consists of two β-strands connected by a loop and placed in different sheets in such a way which looks as Greek letter П. Total 70 non-homologous proteins at resolution not less than 2.5Å have been selected for the analysis from 265 suitable structures belonging to sixteen OB-fold super families. We have disclosed two types of П-modules: the fist with the connecting loop containing α-helix, and second one without helix. Entrance of protein chain into second β-sheet is carried out by the same arch with conformation βββαLβp. In most cases, 85 % of total, α-positions are occupied by glycine residue, while at entrance in the loop such residues are absent. Occupancy frequency of П-modules has been obtained in dependence on the loop length. Spatial pathway of structures of all modules are superimposed very well. Structural alignment of amino acid for П-module sequences allows us to determine the key positions of the hydrophobic, hydrophilic, and glycine residues.