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Similar to other substances associated with the activities of honeybees, RJ not only contains nutritive components, such as carbohydrates, proteins, peptides, lipids, vitamins, and mineral salts,\u00a0but also represents a natural ingredient with cosmetic and health\u2010promoting properties. RJ is characterized by remarkable multifunctionality, possessing numerous biological activities. Although this multifunctionality of RJ can be considered as a consequence of its complex nature, many proteins and peptides in RJ are polyfunctional entities themselves. In this article, we show that RJ proteins contain different levels of intrinsic disorder, have sites of post\u2010translational modifications, can be found in multiple isoforms, and many of them possess disorder\u2010based binding sites, suggesting that the conformational ensembles of the RJ proteins might undergo change as a result of their interaction with specific binding partners. All these observations suggest that the multifunctionality of proteins and peptides from RJ is determined by their structural heterogeneity and polymorphism, and serve as an illustration of the protein structure\u2010function continuum concept.<\/jats:p>","DOI":"10.1002\/pmic.202000237","type":"journal-article","created":{"date-parts":[[2021,1,19]],"date-time":"2021-01-19T02:22:36Z","timestamp":1611022956000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["Multifunctionality and intrinsic disorder of royal jelly proteome"],"prefix":"10.1002","volume":"21","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4037-5857","authenticated-orcid":false,"given":"Vladimir N.","family":"Uversky","sequence":"first","affiliation":[{"name":"Department of Biological Sciences, Faculty of Sciences King Abdulaziz University  Jeddah 21589 80203 Saudi Arabia"},{"name":"Protein Research Group Institute for Biological Instrumentation of 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