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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 ...
Role of Grp 75 Chaperone Folding Machinery in the Maintenance of Mitochondrial Protien Quality Control
(2018-04-03)
My research focuses on understanding the importance of human mitochondrial Hsp70 (Grp75) chaperone machinery for the maintenance of protein quality control inside the mitochondrial matrix. The investigations carried out ...
Diaminopropionate Ammonia Lyase : Characterization, Unfolding And Mechanism Of Inhibition By Aminooxy Compounds
(2009-03-13)
Diaminopropionate ammonia lyase (DAPAL) which belongs to the class of PLP enzymes is reported only from prokaryotes. It is involved in the removal of two amino groups from its substrate, diaminopropionate, to form ammonia ...