Characterization of pre-molten globule state of yeast iso-1-cytochrome c and its deletants at pH 6.0 and 25 °C

Haque, Md. Anzarul; Ubaid-ullah, Shah; Zaidi, Sobia; Hassan, Md. Imtaiyaz; Islam, Asimul; Batra, Janendra K.; Ahmad, Faizan

doi:10.1016/j.ijbiomac.2014.10.053

Cited by 22 publications

(6 citation statements)

References 92 publications

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“…With native and alkaline conditions, no significant difference in fluorescence intensity was seen (see inset of Figure 3 ). This resulted from the solvent inaccessibility of buried hydrophobic clusters, which prevents the ANS binding [ 44 , 45 ].…”

Section: Resultsmentioning

confidence: 99%

Structural Characterization of Ectodomain G Protein of Respiratory Syncytial Virus and Its Interaction with Heparan Sulfate: Multi-Spectroscopic and In Silico Studies Elucidating Host-Pathogen Interactions

et al. 2021

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The global burden of disease caused by a respiratory syncytial virus (RSV) is becoming more widely recognized in young children and adults. Heparan sulfate helps in attaching the virion through G protein with the host cell membrane. In this study, we examined the structural changes of ectodomain G protein (edG) in a wide pH range. The absorbance results revealed that protein maintains its tertiary structure at physiological and highly acidic and alkaline pH. However, visible aggregation of protein was observed in mild acidic pH. The intrinsic fluorescence study shows no significant change in the λmax except at pH 12.0. The ANS fluorescence of edG at pH 2.0 and 3.0 forms an acid-induced molten globule-like state. The denaturation transition curve monitored by fluorescence spectroscopy revealed that urea and GdmCl induced denaturation native (N) ↔ denatured (D) state follows a two-state process. The fluorescence quenching, molecular docking, and 50 ns simulation measurements suggested that heparan sulfate showed excellent binding affinity to edG. Our binding study provides a preliminary insight into the interaction of edG to the host cell membrane via heparan sulfate. This binding can be inhibited using experimental approaches at the molecular level leading to the prevention of effective host–pathogen interaction.

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Section: Resultsmentioning

confidence: 99%

Structural Characterization of Ectodomain G Protein of Respiratory Syncytial Virus and Its Interaction with Heparan Sulfate: Multi-Spectroscopic and In Silico Studies Elucidating Host-Pathogen Interactions

et al. 2021

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“…In case of biphasic transitions we can also validate two-state mechanism pathway differently by comparing the total Gibbs free energy change of each transition curve associated with N  X  D with that of N  D transition by other probe or denaturant [60]. Here in urea-induced denaturation of HFE, we observed that unfolding of HFE is used to define thestructural integrity of HFE (Fig.…”

Section: Stability Parametersmentioning

confidence: 90%

“…The reason for this observation is the exposure of hydrophobic patches in the X-state; these patches do not exists in the fully unfolded state due to the high flexibility of polypeptide chain and remains screened from the solvent in the native state [14,59,60]. The PMG state identified during the urea-induced denaturation of HFE shows a number of characteristics features, which resembles well with other proteins [60][61][62][63][64]. Our studies also reveal a significant amount of secondary structure, but less than the molten globule state [5].…”

Section: Discussionmentioning

confidence: 99%

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

Khan

Prakash

Haque

et al. 2016

International Journal of Biological Macromolecules

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“…The folding from the readily synthesized unfolded protein at ribosome to the native active state is remarkably fast despite the astronomical number of possible conformations available to polypeptides. All the proposed mechanisms for protein folding, i.e., the framework model, the diffusion-collision model, the nucleation growth mechanism or the hydrophobic collapse model show that when a polypeptide folds into its native state, there is progressive stabilization of partially structured folding intermediates in a hierarchical manner to prevent the polypeptide chain to go through all possible conformations [ 1 – 5 ]. The characterization of the intermediates on folding pathways is very important as they can serve as initiation points of aggregation apparent in a number of diseases.…”

Section: Introductionmentioning

confidence: 99%

Heterogeneity of Equilibrium Molten Globule State of Cytochrome c Induced by Weak Salt Denaturants under Physiological Condition

et al. 2015

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While many proteins are recognized to undergo folding via intermediate(s), the heterogeneity of equilibrium folding intermediate(s) along the folding pathway is less understood. In our present study, FTIR spectroscopy, far- and near-UV circular dichroism (CD), ANS and tryptophan fluorescence, near IR absorbance spectroscopy and dynamic light scattering (DLS) were used to study the structural and thermodynamic characteristics of the native (N), denatured (D) and intermediate state (X) of goat cytochorme c (cyt-c) induced by weak salt denaturants (LiBr, LiCl and LiClO4) at pH 6.0 and 25°C. The LiBr-induced denaturation of cyt-c measured by Soret absorption (Δε 400) and CD ([θ]409), is a three-step process, N ↔ X ↔ D. It is observed that the X state obtained along the denaturation pathway of cyt-c possesses common structural and thermodynamic characteristics of the molten globule (MG) state. The MG state of cyt-c induced by LiBr is compared for its structural and thermodynamic parameters with those found in other solvent conditions such as LiCl, LiClO4 and acidic pH. Our observations suggest: (1) that the LiBr-induced MG state of cyt-c retains the native Met80-Fe(III) axial bond and Trp59-propionate interactions; (2) that LiBr-induced MG state of cyt-c is more compact retaining the hydrophobic interactions in comparison to the MG states induced by LiCl, LiClO4 and 0.5 M NaCl at pH 2.0; and (3) that there exists heterogeneity of equilibrium intermediates along the unfolding pathway of cyt-c as highly ordered (X1), classical (X2) and disordered (X3), i.e., D ↔ X3 ↔ X2 ↔ X1 ↔ N.

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Characterization of pre-molten globule state of yeast iso-1-cytochrome c and its deletants at pH 6.0 and 25 °C

Cited by 22 publications

References 92 publications

Structural Characterization of Ectodomain G Protein of Respiratory Syncytial Virus and Its Interaction with Heparan Sulfate: Multi-Spectroscopic and In Silico Studies Elucidating Host-Pathogen Interactions

Structural Characterization of Ectodomain G Protein of Respiratory Syncytial Virus and Its Interaction with Heparan Sulfate: Multi-Spectroscopic and In Silico Studies Elucidating Host-Pathogen Interactions

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

Heterogeneity of Equilibrium Molten Globule State of Cytochrome c Induced by Weak Salt Denaturants under Physiological Condition

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