(Q44448432)

English

Denaturant-induced equilibrium unfolding of concanavalin A is expressed by a three-state mechanism and provides an estimate of its protein stability

scientific article published in May 2003

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scholarly article

1 reference

Europe PubMed Central

3 December 2017

Denaturant-induced equilibrium unfolding of concanavalin A is expressed by a three-state mechanism and provides an estimate of its protein stability (English)

1 reference

Europe PubMed Central

3 December 2017

author name string

Anindya Chatterjee

1

1 reference

Europe PubMed Central

3 December 2017

Dipak K Mandal

2

1 reference

Europe PubMed Central

3 December 2017

publication date

1 May 2003

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Europe PubMed Central

3 December 2017

Biochimica et Biophysica Acta

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Europe PubMed Central

3 December 2017

1648

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Europe PubMed Central

3 December 2017

1-2

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Europe PubMed Central

3 December 2017

174-183

1 reference

Europe PubMed Central

3 December 2017

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Thermodynamics of lectin-carbohydrate interactions. Titration microcalorimetry measurements of the binding of N-linked carbohydrates and ovalbumin to concanavalin A.

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Thermodynamics of lectin-carbohydrate interactions. Binding of the core trimannoside of asparagine-linked carbohydrates and deoxy analogs to concanavalin A.

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Determination and analysis of urea and guanidine hydrochloride denaturation curves

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How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stability

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Unfolding and refolding of Escherichia coli chaperonin GroES is expressed by a three-state model

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Stability and reconstitution of pyruvate oxidase from lactobacillus plantarum: Dissection of the stabilizing effects of coenzyme binding and subunit interaction

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Folding and association of oligomeric and multimeric proteins

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Analysis of equilibrium dissociation and unfolding in denaturants of soybean agglutinin and two of its derivatives

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Alkali and urea induced conformation changes in concanavalin A

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7 January 2021

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Denaturation of concanavalin A by urea at acid pH

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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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Identifiers

10.1016/S1570-9639(03)00120-1

1 reference

Europe PubMed Central

3 December 2017

1 reference

Europe PubMed Central

3 December 2017

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