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231226s2022 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.2c02409
|2 doi
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|a pubmed24n1157.xml
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|a (DE-627)NLM347325351
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|a DE-627
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|a eng
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| 100 |
1 |
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|a Pramanik, Ushasi
|e verfasserin
|4 aut
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| 245 |
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|a Structure and Transition Dynamics of Intrinsically Disordered Proteins Probed by Single-Molecule Spectroscopy
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|c 2022
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|a Date Completed 26.10.2022
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|a Date Revised 15.12.2022
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a 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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|a Journal Article
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|a Review
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|a Intrinsically Disordered Proteins
|2 NLM
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|a Ligands
|2 NLM
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| 700 |
1 |
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|a Nandy, Atanu
|e verfasserin
|4 aut
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1 |
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|a Khamari, Laxmikanta
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Mukherjee, Saptarshi
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 38(2022), 42 vom: 25. Okt., Seite 12764-12772
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|g volume:38
|g year:2022
|g number:42
|g day:25
|g month:10
|g pages:12764-12772
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|u http://dx.doi.org/10.1021/acs.langmuir.2c02409
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