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Thermodynamic Characterization Of Wild Type And Mutants Of The E.coli Periplasmic Binding Proteins LBP, LIVBP, MBP And RBP
(2009-03-13)
Native states of globular proteins typically show stabilization in the range of 5 to
15 kcal/mol with respect to their unfolded states. There has been a considerable progress in the area of protein stability and folding ...
Folding Studies On Peanut Agglutinin : A Lectin With An Unusual Quaternary Structure
(2009-03-04)
The thesis entitled “Folding studies on Peanut Agglutinin: A lectin with an unusual quaternary structure” deals with the several aspects of the folding of the tetrameric legume lectin Peanut Agglutinin ...
Interaction Of Chaperone SecB With Protein Substrates: A Biophysical Study
(Indian Institute of Science, 2006-10-17)
In the cell, as in in vitro, the final conformation of a protein is determined by it's amino acid sequence (1). Some isolated proteins can be denatured and refolded in vitro in absence of extrinsic factors. However, in ...