Structural basis of urea-induced unfolding: Unraveling the folding pathway of hemochromatosis factor E

Khan, Parvez; Prakash, Amresh; Haque, Md. Anzarul; Islam, Asimul; Hassan, Md. Imtaiyaz; Ahmad, Faizan

doi:10.1016/j.ijbiomac.2016.06.055

Cited by 21 publications

(4 citation statements)

References 74 publications

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“…Thereafter, the culture was pelleted down by centrifugation at 3320× g for 20 min at 4 °C. The pellet was resuspended in 20 mM Tris-Cl pH 8.0 buffer for cell lysis using ultrasonication by following the reported method . The insoluble cellular debris was cleared by centrifugation (3320× g for 20 min), and the cleared supernatant was subjected to Ni-NTA chromatography (Qiagen, Germany).…”

Section: Methodsmentioning

confidence: 99%

“…The pellet was resuspended in 20 mM Tris-Cl pH 8.0 buffer for cell lysis using ultrasonication by following the reported method. 35 The insoluble cellular debris was cleared by centrifugation (3320×g for 20 min), and the cleared supernatant was subjected to Ni-NTA chromatography (Qiagen, Germany). Subsequently, bound protein was eluted by elution buffer (20 mM Tris-Cl and 250 mM Imidazole, pH 8.0).…”

Section: ■ Experimental Sectionmentioning

confidence: 99%

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A Fluorescence Resonance Energy Transfer-Based Analytical Tool for Nitrate Quantification in Living Cells

et al. 2020

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Nitrate (NO3 –) is a critical source of nitrogen (N) available to microorganisms and plants. Nitrate sensing activates signaling pathways in the plant system that impinges upon, developmental, molecular, metabolic, and physiological responses locally, and globally. To sustain, the high crop productivity and high nutritional value along with the sustainable environment, the study of rate-controlling steps of a metabolic network of N assimilation through fluxomics becomes an attractive strategy. To monitor the flux of nitrate, we developed a non-invasive genetically encoded fluorescence resonance energy transfer (FRET)-based tool named “FLIP-NT” that monitors the real-time uptake of nitrate in the living cells. The developed nanosensor is suitable for real-time monitoring of nitrate flux in living cells at subcellular compartments with high spatio-temporal resolution. The developed FLIP-NT nanosensor was not affected by the pH change and have specificity for nitrate with an affinity constant (K d) of ∼5 μM. A series of affinity mutants have also been generated to expand the physiological detection range of the sensor protein with varying K d values. It has been found that this sensor successfully detects the dynamics of nitrate fluctuations in bacteria and yeast, without the disruption of cellular organization. This FLIP-NT nanosensor could be a very important tool that will help us to advance the understanding of nitrate signaling.

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Section: Methodsmentioning

confidence: 99%

Section: ■ Experimental Sectionmentioning

confidence: 99%

A Fluorescence Resonance Energy Transfer-Based Analytical Tool for Nitrate Quantification in Living Cells

et al. 2020

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“…MGs of globular proteins are generally obtained by their mild denaturation that can be induced by acid, alkali, low to medium concentrations of chemical denaturants such as urea and GdmHCl, chaotropic salts, moderately high temperature, and, for some proteins, even by low temperature [128][129][130][131][132][133][134][135][136][137][138][139][140][141][142][143][144][145][146][147]. Later studies revealed that in some proteins, an MG can also be induced by various organic solvents [148][149][150][151].…”

Section: How Can One Find Molten Globules and Where Can They Be Found?mentioning

confidence: 99%

Pre-Molten, Wet, and Dry Molten Globules en Route to the Functional State of Proteins

Gupta

Uversky

2023

IJMS

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Transitions between the unfolded and native states of the ordered globular proteins are accompanied by the accumulation of several intermediates, such as pre-molten globules, wet molten globules, and dry molten globules. Structurally equivalent conformations can serve as native functional states of intrinsically disordered proteins. This overview captures the characteristics and importance of these molten globules in both structured and intrinsically disordered proteins. It also discusses examples of engineered molten globules. The formation of these intermediates under conditions of macromolecular crowding and their interactions with nanomaterials are also reviewed.

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“…MGs of globular proteins are generally obtained by their mild denaturation that can be induced by acid, alkali, low to medium concentrations of chemical denaturants, such as urea and GdmHCl, chaotropic salts, moderately high temperature, and, for some proteins, even by low temperature [128][129][130][131][132][133][134][135][136][137][138][139][140][141][142][143][144][145][146][147]. Later studies revealed that in some proteins, MG can be also induced by various organic solvents [148][149][150][151].…”

Section: How One Can Find Molten Globules and Where They Can Be Found?mentioning

confidence: 99%

Pre-Molten, Wet, and Dry Molten Globules <i>En Route</i> to the Functional State of Proteins

Gupta¹,

Uversky²

2023

Preprint

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Transition between the unfolded and native states of the ordered globular proteins is accompanied by accumulation of several intermediates, such as pre-molten globule, wet molten globule, and dry molten globule. Structurally equivalent conformations can serve as native functional states of intrinsically disordered proteins. This overview captures the characteristics and importance of these molten globules in both structured and intrinsically disordered proteins. It also discusses examples of engineered molten globules. The formation of these intermediates under the conditions of macromolecular crowding and their interactions with nanomaterials are also reviewed.

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Structural basis of urea-induced unfolding: Unraveling the folding pathway of hemochromatosis factor E

Cited by 21 publications

References 74 publications

A Fluorescence Resonance Energy Transfer-Based Analytical Tool for Nitrate Quantification in Living Cells

A Fluorescence Resonance Energy Transfer-Based Analytical Tool for Nitrate Quantification in Living Cells

Pre-Molten, Wet, and Dry Molten Globules en Route to the Functional State of Proteins

Pre-Molten, Wet, and Dry Molten Globules <i>En Route</i> to the Functional State of Proteins

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