(Q34322742)

English

Legume lectin family, the 'natural mutants of the quaternary state', provide insights into the relationship between protein stability and oligomerization

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scholarly article

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Europe PubMed Central

PubMed publication ID

1 August 2017

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Europe PubMed Central

Legume lectin family, the 'natural mutants of the quaternary state', provide insights into the relationship between protein stability and oligomerization (English)

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Europe PubMed Central

PubMed publication ID

1 August 2017

author name string

V R Srinivas

1

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Europe PubMed Central

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1 August 2017

G B Reddy

2

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Europe PubMed Central

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1 August 2017

N Ahmad

3

1 reference

Europe PubMed Central

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1 August 2017

C P Swaminathan

4

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Europe PubMed Central

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1 August 2017

N Mitra

5

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Europe PubMed Central

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1 August 2017

A Surolia

6

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Europe PubMed Central

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1 August 2017

language of work or name

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publication date

1 August 2001

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Europe PubMed Central

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1 August 2017

Biochimica et Biophysica Acta

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Europe PubMed Central

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1 August 2017

1527

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Europe PubMed Central

PubMed publication ID

1 August 2017

3

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Europe PubMed Central

PubMed publication ID

1 August 2017

102-111

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

Matching speed and stability

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Variability in quaternary association of proteins with the same tertiary fold: a case study and rationalization involving legume lectins

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Structures of the lectin IV of Griffonia simplicifolia and its complex with the Lewis b human blood group determinant at 2.0 A resolution

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Crystal structure of peanut lectin, a protein with an unusual quaternary structure

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

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Differential scanning calorimetric studies of the glycoprotein, winged bean acidic lectin, isolated from the seeds of Psophocarpus tetrogonolobus

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Thermal stability and mode of oligomerization of the tetrameric peanut agglutinin: a differential scanning calorimetry study.

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Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose

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Cloning and sequencing of winged bean (Psophocarpus tetragonolobus) basic agglutinin (WBA I): presence of second glycosylation site and its implications in quaternary structure

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Carbohydrate specificity and quaternary association in basic winged bean lectin: X-ray analysis of the lectin at 2.5 A resolution

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Carbohydrate specificity and salt-bridge mediated conformational change in acidic winged bean agglutinin

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Thermodynamic characterization of the conformational stability of the homodimeric protein, pea lectin

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The primary structure of the acidic lectin from winged bean (Psophocarpus tetragonolobus): insights in carbohydrate recognition, adenine binding and quaternary association

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Identifiers

10.1016/S0304-4165(01)00153-2

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

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