Intrinsically Disordered Proteins (IDPs): Experimental and Computational Approaches in Drug Discovery
Journal Title: Drug Designing & Intellectual Properties International Journal - Year 2018, Vol 1, Issue 5
Abstract
Soluble proteins may consist of globular units and non-globular units. Globular units are composed of regular secondary structure elements whereas the non-globular units are composed of disordered, unstructured, and flexible regions without regular secondary structure elements [1]. Recently it is well known that many functionally important protein segments occur outside of globular units [2,3]. Intrinsically Disordered Proteins (IDPs) (also known as intrinsically unstructured, unfolded, natively disordered or rheomorphic proteins) lack a well-defined 3D structure and exhibit a multitude of conformations that dynamically change over time and population [4]. Many proteins cannot be over-expressed, purified or crystallized. Native conformational disorder of proteins is one of the main obstacles facing structural biology analyses. Moreover, in structural genomics initiatives, it is becoming increasingly important to identify Intrinsically Disordered Proteins during the target selection process [5,6]. No commonly agreed definition of Intrinsically Disordered Proteins exists. AIDPs can be either completely unfolded or comprise both folded and unfolded segments” [7]. While completely unfolded proteins carry out their function by means of regions that lack specific 3D structure and exists as an ensemble of flexible molecules, in partially unfolded proteins only localized regions lack organized structure.
Authors and Affiliations
Suresh Kumar
Keywords
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- EP ID EP587284
- DOI 10.32474/DDIPIJ.2018.01.000123
- Views 135
- Downloads 0
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