Intrinsically Disordered Proteins (IDPs): From Structure to Mechanism and Function
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".
Deadline for manuscript submissions: closed (20 May 2026) | Viewed by 2260
Editor
Interests: IDP; NMR; pre-structured; PreSMo; target binding
Special Issue Information
Dear Colleagues,
Approximately three decades ago, a fascinating notion regarding unstructured proteins which, at the time, was hard to fully appreciate, was put forward proposing that proteins can be unstructured, i.e., not forming stable three-dimensional structures under non-denaturing conditions, yet can be functional. Predictions have shown that tens of thousands of such proteins called intrinsically disordered/unstructured proteins (IDPs/IUPs) now may exist, while hundreds of them have been characterized experimentally. To be functional, proteins must be able to interact with their targets such as proteins, nucleic acids, membranes, small molecules, and so on. This is also true of IDPs. Early on, the unstructured nature of IDPs was rather hastily interpreted, as if these proteins in the target-free state were totally unstructured, having no traces of structural elements. An argument was then formed that the target binding of IDPs should conform to a full induced fit mechanism where IDP target binding involves a completely unstructured segment of an IDP which forms a stable secondary structure, e.g., a helix, only upon binding. On the other hand, it has been proven thoroughly and quantitatively by NMR methods since 2000 that IDPs are prepopulated (10~90%) with transient secondary structures termed pre-structured motifs (PreSMos). The structural state of IDPs resembles that of an initial folding intermediate. The PreSMos are formed by core hydrophobic residues, which are hot spots recognized by target. Upon target binding, an IDP undergoes an intermolecular (not intramoleular) folding process that prevents the exposure of hydrophobic surfaces and results in formation of stable secondary structures by transient PreSMos. The existence of PreSMos suggests that IDP-target binding should follow a concerted mechanism involving conformational selection followed by induced fit.
Prof. Dr. Kyouhoon Han
Guest Editor
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Keywords
- IDP
- NMR
- completely unstructured
- pre-structured
- PreSMo
- target binding
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