Dynamic light scattering study of peanut agglutinin: size, shape and urea denaturation (Q47300961)

13 January 2018

title

Dynamic light scattering study of peanut agglutinin: size, shape and urea denaturation (English)

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13 January 2018

author name string

Sagarika Dev

series ordinal

1

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13 January 2018

Avadhesha Surolia

series ordinal

2

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13 January 2018

publication date

1 December 2006

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13 January 2018

published in

Journal of Biosciences

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13 January 2018

volume

31

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13 January 2018

issue

5

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13 January 2018

page(s)

551-556

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13 January 2018

https://scigraph.springernature.com/pub.10.1007/bf02708406

exact match

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cites work

Analysis of the peanut agglutinin molten globule-like intermediate by limited proteolysis.

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Crossref

https://api.crossref.org/works/10.1007%2FBF02708406

Molten globule-like state of peanut lectin monomer retains its carbohydrate specificity. Implications in protein folding and legume lectin oligomerization

21 January 2018

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Alpha-Lactalbumin: compact state with fluctuating tertiary structure?

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‘Molten‐globule state’: a compact form of globular proteins with mobile side‐chains

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Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactose complex

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Conformational stability of globular proteins

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The macromolecular properties of peanut agglutinin

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Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbumin

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Thermodynamic analysis of three state denaturation of Peanut Agglutinin.

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Conformational stability of legume lectins reflect their different modes of quaternary association: solvent denaturation studies on concanavalin A and winged bean acidic agglutinin.

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From two-state to three-state: the effect of the P61A mutation on the dynamics and stability of the factor for inversion stimulation results in an altered equilibrium denaturation mechanism

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Study of thermal denaturation of lysozyme and other glubular proteins by light-scattering spectroscopy

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Structural plasticity of peanut lectin: an X-ray analysis involving variation in pH, ligand binding and crystal structure

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Molten globule intermediates and protein folding

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Predissociated Dimers and Molten Globule Monomers in the Equilibrium Unfolding of Yeast Glutathione Reductase

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The purification, composition, and specificity of the anti-T lectin from peanut (Arachis hypogaea).

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The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure.

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Unfolding studies on soybean agglutinin and concanavalin a tetramers: a comparative account

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2,2,2-Trifluoroethanol-Induced structural change of peanut agglutinin at different pH: A comparative account

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Using nuclear magnetic resonance spectroscopy to study molten globule states of proteins

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Resting places on folding pathways

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Identifiers

DOI

10.1007/BF02708406

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13 January 2018

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13 January 2018