Solution and in silico studies on the recombinant lectin from Cicer arietinum seeds

► Cloning and expression of the plant lectin gene into active protein in Escherichia coli. ► Thermo-labile protein showing rapid structural changes from 50 to 55°C. ► Unfolding followed by dissociation of the dimer in presence of GdnHCl. ► Reorientation of trp microenvironment in low concentration o...

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Veröffentlicht in:	International journal of biological macromolecules 2013-05, Vol.56, p.149-155
Hauptverfasser:	Wakankar, Madhurima S., Krishnasastry, Musti V., Jaokar, Tulika M., Patel, Krunal A., Gaikwad, Sushama M.
Format:	Artikel
Sprache:	eng
Schlagworte:	Aggregation Animals bioinformatics BL21-CodonPlus (DE3)-RIL cells Cicer - chemistry Cicer - drug effects Cicer arietinum Cicer lectin Cloning, Molecular Computer Simulation denaturation dissociation Escherichia coli Guanidine - pharmacology Homology model hydrophobicity lectins Lectins - chemistry Lectins - isolation & purification Models, Molecular Molecular Sequence Data Protein Denaturation - drug effects Protein Refolding - drug effects Protein Structure, Secondary Protein Unfolding - drug effects Rabbits Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Reproducibility of Results seeds Seeds - chemistry Solutions Spectrometry, Fluorescence Steady-state and time resolved fluorescence Structural Homology, Protein surface proteins Temperature tryptophan Tryptophan - metabolism Unfolding
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