Implication of Molten Globule on the Function and Toxicity of a Protein

Dhaliwal, Harkiran Preet Kaur; Kumar, Raj; Singh, Bal Ram

doi:10.1007/978-3-319-43540-4_4

Cited by 2 publications

(3 citation statements)

References 206 publications

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“…Proteins are shown to adopt varying different conformations during folding/unfolding. These conformations, generally called molten globules, not only assist the protein to take native fold, but can also impart a functional advantage to the molecule (18,21). Thus, understanding molecular details of these conformations is both interesting and important.…”

Section: Discussionmentioning

confidence: 99%

“…Reports are available that present a detailed examination of the folding intermediate of a protein under physiological buffer conditions (14,15). Besides being the folding intermediates, MGs are also known to hold functional significance and are known to carry out biological functions (16)(17)(18)(19)(20)(21). Some notable examples include the functional role in protein-ligand interaction (22), recognition of chaperones (23), cellular toxins (24), enzymatic roles (25), translocation across membrane (26) and genetic disease (27).…”

Section: Introductionmentioning

confidence: 99%

“…Some notable examples include the functional role in protein-ligand interaction (22), recognition of chaperones (23), cellular toxins (24), enzymatic roles (25), translocation across membrane (26) and genetic disease (27). This suggests that MG may not only be a folding intermediate of protein, but also a state adopted by the protein to perform a specific function inside cell (21).…”

Section: Introductionmentioning

confidence: 99%

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Identification and Characterization of an Inside-Out Folding Intermediate of T4 Phage Sliding Clamp

Singh

Jain

2017

Biophysical Journal

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Protein folding process involves formation of transiently occurring intermediates that are difficult to isolate and characterize. It is both necessary and interesting to characterize the structural conformations adopted by these intermediates, also called molten globules (MG), to understand protein folding. Here, we investigated the equilibrium (un)folding intermediate state of T4 phage gene product 45 (gp45, also known as DNA polymerase processivity factor or sliding clamp) obtained during chemical denaturation. We show that gp45 undergoes substantial conformational rearrangement during unfolding and forms an expanded dry-MG. By monitoring the fluorescence of tryptophans that were strategically introduced at various sites, we demonstrate that the urea-treated molecule has its surface residues flip inside the core, and closely placed residues move farther. We were also able to isolate and purify the MG form of gp45 in native condition (i.e., nondenaturing buffer, at physiological pH and temperature); characteristics of this purified molecule substantially match with urea-treated wild-type gp45. To the best of our knowledge, this is one of the few reports that demonstrate the isolation and purification of a protein folding intermediate in native condition. We believe that our work not only allows us to dissect the process of protein folding, but will also help in the designing of folding inhibitors against sliding clamps to treat a wide variety of diseases from bacterial infection to cancer, due to the vast presence of clamps in all the domains of life.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Identification and Characterization of an Inside-Out Folding Intermediate of T4 Phage Sliding Clamp

Singh

Jain

2017

Biophysical Journal

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Boolean Logic Gate Operation in Bacteriorhodopsin of Purple Membrane Based on a Molten Globule‐like State

Mostafa

2024

ChemPhysChem

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Bacteriorhodopsin (bR) of purple membrane (PM) has increasing technical interests, particularly in photonic devices and bioelectronics. The present work has concerned with monitoring the temperature dependence of passive electric responses in‐plane and out‐of‐plane of the membranes. Based on thermal properties observed orthogonally here for PM, a high‐temperature intermediate of bR has been suggested to populate at around 60 °C, which may be ascribed to a molten globule‐like state. This intermediate has been found to be enclosed between two reversible thermal transitions for PM. Large‐scale turnover in the energy of activation, for these two thermal transitions, occurs steeply at such state at 60 °C, above which does bR reverse the sign of dielectric anisotropy (i.e. crossover) provided the operating frequency should be above the crossover frequency, at which the reversal occurs. No such crossover was found to occur below the crossover frequency, even above the crossover temperature (i.e. 60 °C). Likewise, no such crossover was found to occur below the crossover temperature, even above the crossover frequency. Relying on this reasoning, a logic gate operation may be declared implicating bR for bioelectronics and sense technological relevance. In addition, the results specify “dual frequency” as well as “dual temperature” characteristics to bacteriorhodopsin.

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Implication of Molten Globule on the Function and Toxicity of a Protein

Cited by 2 publications

References 206 publications

Identification and Characterization of an Inside-Out Folding Intermediate of T4 Phage Sliding Clamp

Identification and Characterization of an Inside-Out Folding Intermediate of T4 Phage Sliding Clamp

Boolean Logic Gate Operation in Bacteriorhodopsin of Purple Membrane Based on a Molten Globule‐like State

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