Characterization of Hydroxyl-hydrogen Bond and its Role in Protein Stability and Function
EPrints@IICB
View Archive InfoField | Value | |
Title |
Characterization of Hydroxyl-hydrogen Bond and its Role in Protein Stability and Function
|
|
Creator |
Sen, Sudeshna
|
|
Subject |
Structural Biology & Bioinformatics
|
|
Description |
Hydrogen bonding involving hydroxyl (OH) group has been recognized as playing a fundamental role in determining the structural stability, function and dynamics of many chemical and biological systems. Intramolecular and intermolecular H-bonds provide ample structural stability to proteins and nucleic acids. It also plays an important role in enzyme-catalysis and molecular recognition processes. It is one of the most important noncovalent interactions between substrate and enzyme active site residues. One of our objectives was to investigate the role of hydrogen bonding interaction in ribonuclease A-mediated hydrolysis of RNA. We have chosen ribose, an integral analog of nucleic acid (deoxyribose in DNA and ribose in RNA) as our model compound. We employed deuterium isotope effect to probe the intramolecular and intermolecular H-bonding interactions and to elucidate enzymatic reaction mechanism of RNAse A. We have utilized NMR and Raman spectroscopic methods as a primary tool to determine the strength of H-bond and related thermodynamic parameters in free ribose and in ribonucleotide, uridine monophosphate (UMP). We have also supported our study with extensive density functional theory (DFT) calculations. |
|
Date |
2016-09-23
|
|
Type |
Thesis
NonPeerReviewed |
|
Format |
application/pdf
|
|
Identifier |
http://www.eprints.iicb.res.in/2557/1/Sudeshna_Final_Thesis.pdf
Sen, Sudeshna (2016) Characterization of Hydroxyl-hydrogen Bond and its Role in Protein Stability and Function. PhD thesis, J U. |
|
Relation |
http://www.eprints.iicb.res.in/2557/
|
|