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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 ...
Structure, Stability and Evolution of Multi-Domain Proteins
(2018-04-11)
Analyses of protein sequences from diverse genomes have revealed the ubiquitous nature of multi-domain proteins. They form up to 70% of proteomes of most eukaryotic organisms. Yet, our understanding of protein structure, ...
Topology-based Sequence Design For Proteins Structures And Statistical Potentials Sensitive To Local Environments
(2013-01-17)
Proteins, which regulate most of the biological activities, perform their functions through their unique three-dimensional structures. The folding process of this three dimensional structure from one dimensional sequence ...
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 ...