A Single‐Molecule Approach to Explore the Role of the Solvent Environment in Protein Folding

Tych, Katarzyna M.; Dougan, Lorna

doi:10.1002/9781118523063.ch15

Cited by 3 publications

(2 citation statements)

References 134 publications

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“…In recent years there have been a large number of studies to understand the role of osmolytes on protein mechanical stability. Osmolytes are small organic molecules that can shift the equilibrium between the folded and unfolded states of a protein [217]. So called protecting osmolytes, such as glycerol, sorbitol and sucrose, push the equilibrium towards the folded state of the protein.…”

Section: Role Of Solvent Interactions On Protein Mechanical Stabilitymentioning

confidence: 99%

“…We have recently applied SMFS to manipulate proteins from extremophilic organisms, to gain information about their stability, flexibility and their underlying energy landscapes (figure 29). Using SMFS force extension experiments we measured the mechanical stability of the cold shock protein TmCsp from the hyperthermophilic organism Thermatoga maritima in the temperature range of 5-40 °C [217]. We showed that the mechanical signature of TmCsp is maintained over the entire temperature range and observed temperature-dependent changes in features of the unfolding energy landscape, by studying the pulling speed depend ence of the unfolding force with temperature in combination with Monte Carlo simulations.…”

Section: Smfs Studies Of Proteinsmentioning

confidence: 99%

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The physics of pulling polyproteins: a review of single molecule force spectroscopy using the AFM to study protein unfolding

2016

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One of the most exciting developments in the field of biological physics in recent years is the ability to manipulate single molecules and probe their properties and function. Since its emergence over two decades ago, single molecule force spectroscopy has become a powerful tool to explore the response of biological molecules, including proteins, DNA, RNA and their complexes, to the application of an applied force. The force versus extension response of molecules can provide valuable insight into its mechanical stability, as well as details of the underlying energy landscape. In this review we will introduce the technique of single molecule force spectroscopy using the atomic force microscope (AFM), with particular focus on its application to study proteins. We will review the models which have been developed and employed to extract information from single molecule force spectroscopy experiments. Finally, we will end with a discussion of future directions in this field.

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Section: Role Of Solvent Interactions On Protein Mechanical Stabilitymentioning

confidence: 99%

Section: Smfs Studies Of Proteinsmentioning

confidence: 99%

The physics of pulling polyproteins: a review of single molecule force spectroscopy using the AFM to study protein unfolding

2016

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The effect of deuteration on the keto–enol equilibrium and photostability of the sunscreen agent avobenzone

Murphy

Staton²,

Rawal

et al. 2020

Photochem Photobiol Sci

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H/D Isotope Effects in Keto-Enol Tautomerism of β-Dicarbonyl Compounds —Importance of Nuclear Quantum Effects of Hydrogen Nuclei—

Udagawa

Murphy

Darwish

et al. 2021

Bulletin of the Chemical Society of Japan

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Deuterium isotope effects in the keto-enol tautomerism of β-dicarbonyl compounds (malonaldehyde, acetylacetone, dibenzoylmethane, and avobenzone) have been studied using a B3LYP+D functional level of multi-component density functional theory (MC_DFT), which can directly take nuclear quantum effects (NQEs) of the hydrogen nuclei into account. We clearly show that the keto-enol energy difference becomes smaller by deuterium substitution, which is in reasonable agreement with the corresponding experimental evidence. Our MC_DFT study also reveals the hydrogen/deuterium (H/D) isotope effect in geometries and shows that the deuterium substitution weakens the intramolecular hydrogen-bonded interaction in the enol form. Direct treatment of NQEs of hydrogen nuclei via the MC_DFT method is essential for analyzing the H/D isotope effect in keto-enol tautomerism of β-dicarbonyl compounds. Such isotope effects cannot be reproduced in the conventional DFT scheme with harmonic zero-point vibrational corrections.

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A Single‐Molecule Approach to Explore the Role of the Solvent Environment in Protein Folding

Cited by 3 publications

References 134 publications

The physics of pulling polyproteins: a review of single molecule force spectroscopy using the AFM to study protein unfolding

The physics of pulling polyproteins: a review of single molecule force spectroscopy using the AFM to study protein unfolding

The effect of deuteration on the keto–enol equilibrium and photostability of the sunscreen agent avobenzone

H/D Isotope Effects in Keto-Enol Tautomerism of β-Dicarbonyl Compounds —Importance of Nuclear Quantum Effects of Hydrogen Nuclei—

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