Differing structural characteristics of molten globule intermediate of peanut lectin in urea and guanidine-HCl

Ghosh, Goutam; Mandal, Dipak K.

doi:10.1016/j.ijbiomac.2012.05.010

Cited by 10 publications

(3 citation statements)

References 38 publications

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“…Hence, the purified protein was confirmed as ConA ( Figure 2B). 29,30 Additionally, the FT-IR spectrum of native ConA showed a major peak at 1636 cm −1 , corresponding to native β-sheets in proteins ( Figure 2A); the crystal structure of ConA has been previously shown to contain predominantly β-sheets. 31 Other important peaks were also observed at 1658 and 1696 cm −1 , corresponding to turns that connect stranded sheets to each other.…”

Section: Native Concanavalin Amentioning

confidence: 81%

Chaotropes trigger conformational rearrangements differently in Concanavalin A

et al. 2017

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Concanavalin A (ConA) is a plant lectin having industrial and biological applications. Concanavalin A changes conformation upon exposure to different stress conditions, like exposure to sodium dodecyl sulphate, guanidine hydrochloride, varying hydronium ion potential, etc. The conformational changes were studied using circular dichroism spectroscopy and the structural rigidity of ConA was explored using fluorescence spectroscopy, taking tryptophan as an intrinsic and 8-anilino-1-naphthalenesulfonic acid as an extrinsic fluorescence probes, in different stress conditions. ConA loses the quaternary structure in all the studied stress conditions, which further leads to denaturation of the protein. However, the mechanism of denaturation varied with the studied conditions, like different SDS concentrations and hydronium ion potentials, wherein the protein undergoes a conformational rearrangement from β-sheet to α-helix. Moreover, GdnHCl triggered complete denaturation of ConA into a predominantly random coil conformation. The results suggested that denaturation of ConA follows different pathways depending on the chemical properties and concentrations of the denaturants used.

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Section: Native Concanavalin Amentioning

confidence: 81%

Chaotropes trigger conformational rearrangements differently in Concanavalin A

et al. 2017

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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.

show abstract

Differing structural characteristics of molten globule intermediate of peanut lectin in urea and guanidine-HCl

Cited by 10 publications

References 38 publications

Chaotropes trigger conformational rearrangements differently in Concanavalin A

Chaotropes trigger conformational rearrangements differently in Concanavalin A

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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