smFRET and DEER Distance Measurements as Applied to Disordered and Structured Proteins

Weninger, Keith; Qiu, Ruoyi; Ou, Erkang; Milikisiyants, Sergey; Sanabria, Hugo; Smirnova, Tatyana I.

doi:10.1016/j.bpj.2015.11.2987

Cited by 2 publications

(2 citation statements)

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“…The FRET efficiency of many individual molecules has been calculated and the extent of folding obtained according to the histogram of the signal. Consequently, heterogeneous structures were divided and the abundance change was tracked through time ranging from microseconds to seconds [ 73 ]. The strategy of sample dispersing (i.e., diffusing in solution or tethered on substrates) is chosen based on the molecular characters for various purposes and care should be taken respectively on experimental design.…”

Section: Investigating the Structural Changes Under Various Circumstancesmentioning

confidence: 99%

Single-Molecular Förster Resonance Energy Transfer Measurement on Structures and Interactions of Biomolecules

et al. 2021

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Single-molecule Förster resonance energy transfer (smFRET) inherits the strategy of measurement from the effective “spectroscopic ruler” FRET and can be utilized to observe molecular behaviors with relatively high throughput at nanometer scale. The simplicity in principle and configuration of smFRET make it easy to apply and couple with other technologies to comprehensively understand single-molecule dynamics in various application scenarios. Despite its widespread application, smFRET is continuously developing and novel studies based on the advanced platforms have been done. Here, we summarize some representative examples of smFRET research of recent years to exhibit the versatility and note typical strategies to further improve the performance of smFRET measurement on different biomolecules.

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Section: Investigating the Structural Changes Under Various Circumstancesmentioning

confidence: 99%

Single-Molecular Förster Resonance Energy Transfer Measurement on Structures and Interactions of Biomolecules

et al. 2021

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“…Conformational switching occurs over a wide range of timescales, ranging from very slow processes lasting for seconds down to microsecond timescales [43]. To explain this, a scale-free approach is needed.…”

Section: Theoretical Framework For Understanding Idp Conformationamentioning

confidence: 99%

Spontaneous Switching among Conformational Ensembles in Intrinsically Disordered Proteins

et al. 2019

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The common conception of intrinsically disordered proteins (IDPs) is that they stochastically sample all possible configurations driven by thermal fluctuations. This is certainly true for many IDPs, which behave as swollen random coils that can be described using polymer models developed for homopolymers. However, the variability in interaction energy between different amino acid sequences provides the possibility that some configurations may be strongly preferred while others are forbidden. In compact globular IDPs, core hydration and packing density can vary between segments of the polypeptide chain leading to complex conformational dynamics. Here, we describe a growing number of proteins that appear intrinsically disordered by biochemical and bioinformatic characterization but switch between restricted regions of conformational space. In some cases, spontaneous switching between conformational ensembles was directly observed, but few methods can identify when an IDP is acting as a restricted chain. Such switching between disparate corners of conformational space could bias ligand binding and regulate the volume of IDPs acting as structural or entropic elements. Thus, mapping the accessible energy landscape and capturing dynamics across a wide range of timescales are essential to recognize when an IDP is acting as such a switch.

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smFRET and DEER Distance Measurements as Applied to Disordered and Structured Proteins

Cited by 2 publications

References 0 publications

Single-Molecular Förster Resonance Energy Transfer Measurement on Structures and Interactions of Biomolecules

Single-Molecular Förster Resonance Energy Transfer Measurement on Structures and Interactions of Biomolecules

Spontaneous Switching among Conformational Ensembles in Intrinsically Disordered Proteins

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