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8-Anilinonaphthalene-1-Sulfonic Acid

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Shridhar K Sathe – One of the best experts on this subject based on the ideXlab platform.

  • interactions with 8 anilinonaphthalene 1 sulfonic Acid ans and surface hydrophobicity of black gram vigna mungo phaseolin
    Journal of Food Science, 2018
    Co-Authors: Maithili Deshpande, Shridhar K Sathe

    Abstract:

    Surface hydrophobicity (SH) properties of the trimeric storage protein phaseolin (black gram phaseolin [BGP]) of black gram (Vigna mungo) were investigated using 8‐anilinonaphthalene‐1‐sulfonate (ANS) as an extrinsic fluorescent probe. The emission maxima of fluorescence spectra of BGP:ANS complex were blue‐shifted to 455 nm as compared to 515 nm for the free ANS. Saturation binding occurred at a dye‐to‐protein ratio of about 30:1. The quantum yield of the complex increased with increasing ionic strength. The Kdvalues were 1.7 × 10−5and 1.37 × 10−5M using fractional occupancy and Scatchard analysis, respectively. Analysis of the binding data using Klotz plot revealed 4 binding sites/protomer. SH of BGP was 48%, which rapidly decreased due to the perturbation of the binding sites as the protein unfolded in GdnHCl and urea. By varying processing conditions, it may be possible to alter the surface exposure of SH of BGP to extend its applications in novel food products with desired textural attributes. Varying solvent and/or processing conditions can assist to modulate the surface hydrophobicity of functional legume proteins to achieve desired textural properties in the end product.

  • Interactions with 8‐Anilinonaphthalene‐1‐sulfonic Acid (ANS) and Surface Hydrophobicity of Black Gram (Vigna mungo) Phaseolin
    Journal of food science, 2018
    Co-Authors: Maithili Deshpande, Shridhar K Sathe

    Abstract:

    Surface hydrophobicity (SH) properties of the trimeric storage protein phaseolin (black gram phaseolin [BGP]) of black gram (Vigna mungo) were investigated using 8‐anilinonaphthalene‐1‐sulfonate (ANS) as an extrinsic fluorescent probe. The emission maxima of fluorescence spectra of BGP:ANS complex were blue‐shifted to 455 nm as compared to 515 nm for the free ANS. Saturation binding occurred at a dye‐to‐protein ratio of about 30:1. The quantum yield of the complex increased with increasing ionic strength. The Kdvalues were 1.7 × 10−5and 1.37 × 10−5M using fractional occupancy and Scatchard analysis, respectively. Analysis of the binding data using Klotz plot revealed 4 binding sites/protomer. SH of BGP was 48%, which rapidly decreased due to the perturbation of the binding sites as the protein unfolded in GdnHCl and urea. By varying processing conditions, it may be possible to alter the surface exposure of SH of BGP to extend its applications in novel food products with desired textural attributes. Varying solvent and/or processing conditions can assist to modulate the surface hydrophobicity of functional legume proteins to achieve desired textural properties in the end product.

Maithili Deshpande – One of the best experts on this subject based on the ideXlab platform.

  • interactions with 8 anilinonaphthalene 1 sulfonic Acid ans and surface hydrophobicity of black gram vigna mungo phaseolin
    Journal of Food Science, 2018
    Co-Authors: Maithili Deshpande, Shridhar K Sathe

    Abstract:

    Surface hydrophobicity (SH) properties of the trimeric storage protein phaseolin (black gram phaseolin [BGP]) of black gram (Vigna mungo) were investigated using 8‐anilinonaphthalene‐1‐sulfonate (ANS) as an extrinsic fluorescent probe. The emission maxima of fluorescence spectra of BGP:ANS complex were blue‐shifted to 455 nm as compared to 515 nm for the free ANS. Saturation binding occurred at a dye‐to‐protein ratio of about 30:1. The quantum yield of the complex increased with increasing ionic strength. The Kdvalues were 1.7 × 10−5and 1.37 × 10−5M using fractional occupancy and Scatchard analysis, respectively. Analysis of the binding data using Klotz plot revealed 4 binding sites/protomer. SH of BGP was 48%, which rapidly decreased due to the perturbation of the binding sites as the protein unfolded in GdnHCl and urea. By varying processing conditions, it may be possible to alter the surface exposure of SH of BGP to extend its applications in novel food products with desired textural attributes. Varying solvent and/or processing conditions can assist to modulate the surface hydrophobicity of functional legume proteins to achieve desired textural properties in the end product.

  • Interactions with 8‐Anilinonaphthalene‐1‐sulfonic Acid (ANS) and Surface Hydrophobicity of Black Gram (Vigna mungo) Phaseolin
    Journal of food science, 2018
    Co-Authors: Maithili Deshpande, Shridhar K Sathe

    Abstract:

    Surface hydrophobicity (SH) properties of the trimeric storage protein phaseolin (black gram phaseolin [BGP]) of black gram (Vigna mungo) were investigated using 8‐anilinonaphthalene‐1‐sulfonate (ANS) as an extrinsic fluorescent probe. The emission maxima of fluorescence spectra of BGP:ANS complex were blue‐shifted to 455 nm as compared to 515 nm for the free ANS. Saturation binding occurred at a dye‐to‐protein ratio of about 30:1. The quantum yield of the complex increased with increasing ionic strength. The Kdvalues were 1.7 × 10−5and 1.37 × 10−5M using fractional occupancy and Scatchard analysis, respectively. Analysis of the binding data using Klotz plot revealed 4 binding sites/protomer. SH of BGP was 48%, which rapidly decreased due to the perturbation of the binding sites as the protein unfolded in GdnHCl and urea. By varying processing conditions, it may be possible to alter the surface exposure of SH of BGP to extend its applications in novel food products with desired textural attributes. Varying solvent and/or processing conditions can assist to modulate the surface hydrophobicity of functional legume proteins to achieve desired textural properties in the end product.

Samrat Mukhopadhyay – One of the best experts on this subject based on the ideXlab platform.

  • Dynamics and dimension of an amyloidogenic disordered state of human β_2-microglobulin
    European Biophysics Journal, 2013
    Co-Authors: Dominic Narang, Pushpender K. Sharma, Samrat Mukhopadhyay

    Abstract:

    Human β_2-microglobulin (β_2m) aggregation is implicated in dialysis-related amyloidosis. Previously, it has been shown that β_2m adopts an ensemble of partially unfolded states at low pH. Here we provide detailed structural and dynamical insights into the Acid unfolded and yet compact state of β_2m at pH 2.5 using a host of fluorescence spectroscopic tools. These tools allowed us to investigate protein conformational dynamics at low micromolar protein concentrations in an amyloid-forming condition. Our equilibrium fluorescence data in combination with circular dichroism data provide support in favor of progressive structural dissolution of β_2m with lowering pH. The Acid unfolded intermediate at pH 2.5 has high 8-anilinonaphthalene, 1-sulfonic Acid (ANS)-binding affinity and is devoid of significant secondary structural elements. Using fluorescence lifetime measurements, we have been able to monitor the conformational transition during the pH transition from the native to the compact disordered state. Additionally, using time-resolved fluorescence anisotropy measurements, we have been able to distinguish this compact disordered state from the canonical denatured state of the protein by identifying unique dynamic signatures pertaining to the segmental chain mobility. Taken together, our results demonstrate that β_2m at pH 2.5 adopts a compact noncanonical unfolded state resembling a collapsed premolten globule state. Additionally, our stopped-flow fluorescence kinetics results provide mechanistic insights into the formation of a compact disordered state from the native form.

  • Dynamics and dimension of an amyloidogenic disordered state of human β2-microglobulin
    European biophysics journal : EBJ, 2013
    Co-Authors: Dominic Narang, Pushpender K. Sharma, Samrat Mukhopadhyay

    Abstract:

    Human β2-microglobulin (β2m) aggregation is implicated in dialysis-related amyloidosis. Previously, it has been shown that β2m adopts an ensemble of partially unfolded states at low pH. Here we provide detailed structural and dynamical insights into the Acid unfolded and yet compact state of β2m at pH 2.5 using a host of fluorescence spectroscopic tools. These tools allowed us to investigate protein conformational dynamics at low micromolar protein concentrations in an amyloid-forming condition. Our equilibrium fluorescence data in combination with circular dichroism data provide support in favor of progressive structural dissolution of β2m with lowering pH. The Acid unfolded intermediate at pH 2.5 has high 8-anilinonaphthalene, 1-sulfonic Acid (ANS)-binding affinity and is devoid of significant secondary structural elements. Using fluorescence lifetime measurements, we have been able to monitor the conformational transition during the pH transition from the native to the compact disordered state. Additionally, using time-resolved fluorescence anisotropy measurements, we have been able to distinguish this compact disordered state from the canonical denatured state of the protein by identifying unique dynamic signatures pertaining to the segmental chain mobility. Taken together, our results demonstrate that β2m at pH 2.5 adopts a compact noncanonical unfolded state resembling a collapsed premolten globule state. Additionally, our stopped-flow fluorescence kinetics results provide mechanistic insights into the formation of a compact disordered state from the native form.

  • Kinetics of Surfactant-induced Aggregation of Lysozyme Studied by Fluorescence Spectroscopy
    Journal of Fluorescence, 2011
    Co-Authors: Neha Jain, Mily Bhattacharya, Samrat Mukhopadhyay

    Abstract:

    The study of protein conformational changes in the presence of surfactants and lipids is important in the context of protein folding and misfolding. In the present study, we have investigated the mechanism of the protein conformational change coupled with aggregation leading to size growth of Hen Egg White Lysozyme (HEWL) in the presence of an anionic detergent such as sodium dodecyl sulphate (SDS) in alkaline pH. We have utilized intrinsic protein fluorescence (tryptophan) and extrinsic fluorescent reporters such as 8-Anilinonaphthalene-1-Sulfonic Acid (ANS), dansyl and fluorescein to follow the protein conformational change in real-time. By analyzing the kinetics of fluorescence intensity and anisotropy of multiple fluorescent reporters, we have been able to delineate the mechanism of surfactant-induced aggregation of lysozyme. The kinetic parameters reveal that aggregation proceeds with an initial fast-phase (conformational change) followed by a slow-phase (self-assembly). Our results indicate that SDS, below critical micelle concentration, induces conformational expansion that triggers the aggregation process at a micromolar protein concentration range.