4.6 Article

Structure and Transition Dynamics of Intrinsically Disordered Proteins Probed by Single-Molecule Spectroscopy

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LANGMUIR
卷 38, 期 42, 页码 12764-12772

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AMER CHEMICAL SOC
DOI: 10.1021/acs.langmuir.2c02409

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  1. IISER Bhopal
  2. UGC, Government of India
  3. CSIR, Government of India

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Intrinsically disordered proteins (IDPs) possess unique dynamic characteristics that are difficult to study using traditional methods. Single-molecule measurements provide a better understanding of the conformational transitions of IDPs. These approaches are important for revealing the structural transitions of IDPs and future research directions.
Intrinsically disordered proteins (IDPs) are a class of proteins that do not follow the unanimated perspective of the structure-function paradigm. IDPs enunciate the dynamics of motions which are often difficult to characterize by a particular experimental or theoretical approach. The chameleon nature of the IDPs is a result of an alteration or transition in their conformation upon binding with ligands. Experimental investigations via ensemble-average approaches to probe this randomness are often difficult to synchronize. Thus, to sense the substates of different conformational ensembles of IDPs, researchers have often targeted approaches based on single-molecule measurements. In this Perspective, we will discuss various single-molecule approaches to explore the conformational transitions of IDPs in different scenarios, the outcome, challenges, and future prospects.

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