{"title":"从DisProt数据库中评价具有内在紊乱的蛋白质:概念、生物学重要性和特有特性","authors":"Stephanny M. Alves de Souza, Theo L. F. de Souza","doi":"10.21577/1984-6835.20220008","DOIUrl":null,"url":null,"abstract":"The intrinsic disorder (ID) consists of a feature present in an extensive group of proteins in its totality (IDPs) or only in regions (IDRs). Such feature provides a series of peculiar behaviors that differs from those presented for globular proteins. They are characterized by the absence of a well-defined tridimensional structure, owning high flexibility and conformational entropy, which enables a structural plasticity. In this work, we perform an investigation of different issues involving proteins with ID available in the DisProt database, as well as an extensive literature search to gather information that can help to expand the knowledge about this important group of proteins. Proteins with ID are observed in all kingdoms of life from the simplest to the most complex organisms, where they become more present. They participate of the most diverse biological process, acting mainly in process involving signaling, where the ability to adopt different conformations and bind to different partners becomes fundamental. The ID in proteins is also responsible for the development of diseases and its peculiar structural features bring with them the challenge of developing drugs able to act in these proteins. Different techniques can be applied to analyze structural features presented by these proteins, such as the absence or low structural content, possibility of structural gain, large volume, high solvent exposure and flexibility. With this work, we seek to bring a set of information from the most varied topics involving proteins with ID that can help in the theme disclosure.","PeriodicalId":21315,"journal":{"name":"Revista Virtual de Química","volume":"48 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2022-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Evaluation of Proteins with Intrinsic Disorder from the DisProt Database: Concepts, Biological Importance and Peculiar Characteristics\",\"authors\":\"Stephanny M. Alves de Souza, Theo L. F. de Souza\",\"doi\":\"10.21577/1984-6835.20220008\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The intrinsic disorder (ID) consists of a feature present in an extensive group of proteins in its totality (IDPs) or only in regions (IDRs). Such feature provides a series of peculiar behaviors that differs from those presented for globular proteins. They are characterized by the absence of a well-defined tridimensional structure, owning high flexibility and conformational entropy, which enables a structural plasticity. In this work, we perform an investigation of different issues involving proteins with ID available in the DisProt database, as well as an extensive literature search to gather information that can help to expand the knowledge about this important group of proteins. Proteins with ID are observed in all kingdoms of life from the simplest to the most complex organisms, where they become more present. They participate of the most diverse biological process, acting mainly in process involving signaling, where the ability to adopt different conformations and bind to different partners becomes fundamental. The ID in proteins is also responsible for the development of diseases and its peculiar structural features bring with them the challenge of developing drugs able to act in these proteins. Different techniques can be applied to analyze structural features presented by these proteins, such as the absence or low structural content, possibility of structural gain, large volume, high solvent exposure and flexibility. With this work, we seek to bring a set of information from the most varied topics involving proteins with ID that can help in the theme disclosure.\",\"PeriodicalId\":21315,\"journal\":{\"name\":\"Revista Virtual de Química\",\"volume\":\"48 1\",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2022-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Revista Virtual de Química\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.21577/1984-6835.20220008\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Revista Virtual de Química","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.21577/1984-6835.20220008","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Evaluation of Proteins with Intrinsic Disorder from the DisProt Database: Concepts, Biological Importance and Peculiar Characteristics
The intrinsic disorder (ID) consists of a feature present in an extensive group of proteins in its totality (IDPs) or only in regions (IDRs). Such feature provides a series of peculiar behaviors that differs from those presented for globular proteins. They are characterized by the absence of a well-defined tridimensional structure, owning high flexibility and conformational entropy, which enables a structural plasticity. In this work, we perform an investigation of different issues involving proteins with ID available in the DisProt database, as well as an extensive literature search to gather information that can help to expand the knowledge about this important group of proteins. Proteins with ID are observed in all kingdoms of life from the simplest to the most complex organisms, where they become more present. They participate of the most diverse biological process, acting mainly in process involving signaling, where the ability to adopt different conformations and bind to different partners becomes fundamental. The ID in proteins is also responsible for the development of diseases and its peculiar structural features bring with them the challenge of developing drugs able to act in these proteins. Different techniques can be applied to analyze structural features presented by these proteins, such as the absence or low structural content, possibility of structural gain, large volume, high solvent exposure and flexibility. With this work, we seek to bring a set of information from the most varied topics involving proteins with ID that can help in the theme disclosure.