Intrinsically Disord Proteins. 2013 Nov 07;1(1):e26782. doi: 10.4161/idp.26782. eCollection 2013.
Intrinsically disordered proteins
Vladimir N Uversky
PMID: 28516024 PMCID: PMC5424783 DOI: 10.4161/idp.26782
Intrinsic disorder is everywhere and is inevitable. The non-folding propensity is inherent for numerous natural polypeptide chains, and many functional proteins and protein regions are intrinsically disordered. Furthermore, at particular moments in their life, most notably during their synthesis and degradation, all ordered proteins are at least partially unfolded (disordered). Also, there is a widely spread phenomenon of conditional (functional or transient) disorder, where functions of many ordered proteins require local or even global unfolding of their unique structures. Finally, extrinsic disorder (i.e., intrinsic disorder in functional partners of ordered proteins) should be taken into account too. Therefore, even if a protein is completely devoid of intrinsically disordered regions in its mature form (which is a rather exceptional situation), it faces different forms of disorder (intrinsic, extrinsic, or induced disorder) at all the stages of its functional life, from birth to death. The goal of this article is to briefly introduce this concept of disorder in the lifetime of a protein.
Keywords: intrinsically disordered protein region; nascent polypeptide chain; protein biosynthesis; protein degradation; protein function