The non-uniform early structural response of globular proteins to cold denaturing conditions: A case study with Yfh1

Chatterjee, Prathit; Bagchi, Sayan; Sengupta, Neelanjana

doi:10.1063/1.4901897

Cited by 25 publications

(37 citation statements)

References 91 publications

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“…Observation of the two unfolding temperatures facilitates enormously the calculation of reliable stability curves and of the whole set of thermodynamic parameters. The usefulness of Yfh1 as a tool to investigate unfolding processes is evidenced not only by our subsequent work (Pastore et al, 2007;Sanfelice et al, 2013;Pastore and Temussi, 2017;Alfano et al, 2017) but also by papers from other laboratories (Espinosa et al, 2016;Chatterjee et al, 2014;Bonetti et al, 2014;Aznauryan et al, 2013). We demonstrate that it is possible to sort out which individual single residues yield stability curves consistent with the global unfolding process and that we can obtain valuable information on the process of unfolding from residues that diverge from the average behaviour, Our data also prove directly the distinct mechanisms determining the cold and heat denaturation processes by providing site-specific information on solvent interactions.…”

Section: Discussionmentioning

confidence: 79%

Anatomy of unfolding: The site-specific fold stability of Yfh1 measured by 2D NMR

Puglisi

Pastore

Temussi

2020

Preprint

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Abstract. Most techniques allow detection of protein unfolding either by following the behaviour of single reporters or as an averaged all-or-none process. We recently added 2D NMR spectroscopy to the well-established techniques able to obtain information on the process of unfolding using resonances of residues in the hydrophobic core of a protein. Here, we questioned whether a detailed analysis of the individual stability curves from each resonance could provide additional site-specific information. We used the Yfh1 protein that has the unique feature to undergo both cold and heat denaturation at temperatures above water freezing at low ionic strength. We show that stability curves inconsistent with the average NMR curve from hydrophobic core residues mainly comprise exposed outliers that do nevertheless provide precious information. By monitoring both cold and heat denaturation of individual residues we gain knowledge on the process of cold denaturation and convincingly demonstrate that the two unfolding processes are intrinsically different.

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Section: Discussionmentioning

confidence: 79%

Anatomy of unfolding: The site-specific fold stability of Yfh1 measured by 2D NMR

Puglisi

Pastore

Temussi

2020

Preprint

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“…The possibility that the intensity changes in the HSQCs at low temperature could be solely due to exchange broadening and not to unfolding can however be excluded by the practically perfect agreement between the curves obtained by CD and by NMR (both 1D (Pastore et al, 2007) and 2D (Puglisi et al, 2020)). Cold denaturation of Yfh1 has also been independently confirmed by five independent techniques (Espinosa et al, 2016;Chatterjee et al, 2014;Bonetti et al, 2014;Aznauryan et al, 2013).…”

Section: Data Collection and Preliminary Considerationsmentioning

confidence: 82%

“…We have extensively exploited these properties to gain new insights both on the denatured states of Yfh1 (Adrover et al, 2012) and on the factors that may influence its stability (Martin et al, 2008). The value of Yfh1 as a tool to investigate the unfolding process is evidenced not only by our subsequent work (Sanfelice et al, 2013;Pastore and Temussi, 2017;Sanfelice et al, 2014;Alfano et al, 2017) but also by papers from other laboratories (Espinosa et al, 2016;Chatterjee et al, 2014;Bonetti et al, 2014;Aznauryan et al, 2013).…”

Section: Introductionmentioning

confidence: 98%

Anatomy of unfolding: The site-specific fold stability of Yfh1 measured by 2D NMR

Puglisi

Karunanithy

Hansen

et al. 2021

Preprint

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Most techniques allow detection of protein unfolding either by following the behaviour of single reporters or as an averaged all-or-none process. We recently added 2D NMR spectroscopy to the well-established techniques able to obtain information on the process of unfolding using resonances of residues in the hydrophobic core of a protein. Here, we questioned whether an analysis of the individual stability curves from each resonance could provide additional site-specific information. We used the Yfh1 protein that has the unique feature to undergo both cold and heat denaturation at temperatures above water freezing at low ionic strength. We show that stability curves inconsistent with the average NMR curve from hydrophobic core residues mainly comprise exposed outliers that do nevertheless provide precious information. By monitoring both cold and heat denaturation of individual residues we gain knowledge on the process of cold denaturation and convincingly demonstrate that the two unfolding processes are intrinsically different.

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“…On particle morphology examination using transmission electron microscopy (TEM), each formula showed the shape of spherical particles. The spherical form had a greater solubility in the water phase, so it could increase the biovaibility of medicinal ingredients with low solubility (Chatterjee et al 2014).…”

Section: Transmission Electron Microscopy (Tem)mentioning

confidence: 99%

Effect of Combination Soy Bean Oil and Oleic Acid to Characteristic, Penetration, Physical Stability of Nanostructure Lipid Carrier Resveratrol

Soeratri

Hidayah

Rosita

2019

FMI

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Resveratrol is an antioxidant that can be used as anti-aging. Topical use has several problems because solubility in water is low and unstable to light. This study aimed to evaluate the effect of the combination of soy bean oil and oleic acid liquid lipids on the characteristics, penetration, and stability of resveratrol nanostructured lipid carriers (NLC). Nanostructured lipid carriers (NLC) were made with high shear homogeneous technique. To determine the characterization of NLC, diffraction scanning calorimetry, X-ray diffraction, and Fourier transforms infrared spectrophotometry were used. Examination of the morphological form was carried out with a transmission electron microscope. The particle size and polydispersity index examination were measured by the Delsa Nano™ particle size analyzer, while the efficiency of trapping resveratrol in the NLC system was measured by the dialysis membrane method. Furthermore, the penetration depth test on the skin of mice was done by fluorescence microscope method using rhodamine B markers. Physical stability test was performed by examination of particle size and index polydispersity for 30 days. The formula with liquid soy bean oil and oleic acid liquid lipids improved the characteristics including the effectiveness of entrapment and colloidal stability. However, the formula with soy bean oil and oleic acid combination liquid lipids did not provide better penetration into the skin than the use of single liquid lipids. While the formula with soy bean oil and oleic acid liquid lipids proved to improve the physical stability for 30 days.

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The non-uniform early structural response of globular proteins to cold denaturing conditions: A case study with Yfh1

Cited by 25 publications

References 91 publications

Anatomy of unfolding: The site-specific fold stability of Yfh1 measured by 2D NMR

Anatomy of unfolding: The site-specific fold stability of Yfh1 measured by 2D NMR

Anatomy of unfolding: The site-specific fold stability of Yfh1 measured by 2D NMR

Effect of Combination Soy Bean Oil and Oleic Acid to Characteristic, Penetration, Physical Stability of Nanostructure Lipid Carrier Resveratrol

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