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Title: Role of Protein Microenvironment in Modulating Structure and Function of Cystine Cysteine and Aspartic Acid
Researcher: Bhatnagar, Akshay
Guide(s): Bandyopadhyay, Debashree
Keywords: Biological Science, Protein Microenvironment, Cystine, Cysteine and Aspartic Acid
University: Birla Institute of Technology and Science
Completed Date: 2016
Abstract: Proteins are the functional units of any living system. Proteins play a vital role in many biological reactions like succinate acid dehydrogenase and pyruvate decarboxylase in respiration, Ribulose-1,5-bisphosphate carboxylase/oxygenase in photosynthesis etc. Protein function depends on the three-dimensional arrangement of amino acids. Amino acids are the building blocks of protein newlinestructures. Amino acid form peptide bonds through their main chain atoms to form protein structures. Side chains of amino acids arrange themselves to provide a stable three-dimensional protein structure. This stable structure of the protein has an interior hydrophobic core and a solvent newlineexposed hydrophilic region. However, combination of all the amino acid side chains maintains a heterogeneous dielectric medium (protein microenvironment) within the protein structure. Protein microenvironment is defined here as the three-dimensional arrangement of atoms around a functional group of amino acid side chain. The orientation of neighboring amino acids within a protein microenvironment may dictate the function of an individual amino acid in a particular protein structure. In this thesis, I have reported different microenvironment regions around the disulfide-bridged cystine and cysteine molecules in high-resolution protein crystal structures. Curation of these newlinemicroenvironment regions has shown how microenvironment affects various functions of an amino acid in different protein structure. The conservation of microenvironment around cystine and cysteine molecules that are part of specific functional motifs implies the significance of microenvironment in deciding the functional form of such amino acids in protein structures. I have also studied how the protein microenvironment modulates the side chain protonation state of a titrable amino acid like aspartic acid. Aspartic acid model system has been applied here to newlineunderstand the dielectric nature of different protein microenvironments by comparing it with different solvent systems.
Pagination: 155p.
Appears in Departments:Biological Science

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