What’s in a name? Why these proteins are intrinsically disordered

Abstract

“What’s in a name? That which we call a rose By any other name would smell as sweet.” From “Romeo and Juliet”, William Shakespeare (1594) This article opens a series of publications on disambiguation of the basic terms used in the field of intrinsically disordered proteins. We start from the beginning, namely from the explanation of what the expression “intrinsically disordered protein” actually means and why this particular term has been chosen as the common denominator for this class of proteins characterized by broad structural, dynamic and functional characteristics.

Paradoxes and wonders of intrinsic disorder: Stability of instability

“…[1][2][3][4][5][6][7] Because of their lack of stable structures, exceptional spatiotemporal heterogeneity, outstanding conformational plasticity, ability to be precisely controlled and regulated, and capability to conduct and juggle multiple jobs, intrinsically disordered proteins (IDPs) and hybrid proteins possessing ordered domains and intrinsically disordered protein regions (IDPRs) 8 are specialized in unique biologic functions, [1][2][3][4][5][6][7] which are extending far beyond mostly catalytic activities traditionally assigned to the proteins within the "one gene -one structure -one function" paradigm. 1,3,[10][11][12]18,[39][40][41] In fact, among intrinsic disorder-based biologic functions are regulation of various cellular pathways, binding promiscuity, involvement in diverse signaling processes, and participation in cell protection, protein protection, controlled cell death, and cellular homeostasis.…”

Structural Determinants Allowing Transferase Activity in SENSITIVE TO FREEZING 2, Classified as a Family I Glycosyl Hydrolase

“…Intrinsically disordered regions of proteins have recently been recognized as a separate domain classification (73), which consists of peptides that do not autonomously fold into a single conformation. However, several types of disordered regions have been shown to adopt more specific conformations upon binding to other molecules or post-translational modification (73). Multiple predictors of intrinsic disorder were compared over the full length of SFR2 (Fig.…”

Intrinsic disorder in biomarkers of insulin resistance, hypoadiponectinemia, and endothelial dysfunction among the type 2 diabetic patients

“…[23][24][25][26][27][28][29][30][31][32][33] These intrinsically disordered proteins (IDPs) and hybrid proteins containing both ordered and intrinsically disordered domains/ regions 34 are very common in nature, 31,[35][36][37][38][39] with IDPs constituting significant fractions of all known proteomes, 31,35,36,40,41 and therefore being considered now as an important extension of the protein kingdom. 23,28,32,[42][43][44][45][46] Despite their lack of unique 3D-structures, these proteins are involved in crucial biological processes (such as signaling, regulation, and recognition), [23][24][25][26][27][28][29]31,42,[47][48][49][50][51][52][53]…”