Structural and Functional studies on Isocitrate Lyase and Malate Synthase from Mycobacterium tuberculosis
IR@CDRI: CSIR-Central Drug Research Institute, Lucknow
View Archive Info| Field | Value | |
| Creator |
Kumar, Ranjeet
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| Date |
2014-05-13T09:21:57Z
2014-05-13T09:21:57Z 2009 |
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http://hdl.handle.net/123456789/1238
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| Description |
Guide- Dr. Vinod Bhakuni, PhD Thesis Submitted to JNU, New Delhi in 2009
Proteins drive the nature dynamic machine called life. It has been a challenging bio-molecule to investigate and delineate. The wizardry and diversity they exhibit are enormous. Central dogma ends on this molecule and what begins there on that very point is puzzle called life. Demystifying the architecture of these wonder molecules and appreciating them in the light of laws of chemistry and physics yield information seminal to their structure-function aspects. Their very nature, the diversity, their ability to interact and act in cascade, drive important metabolic pathway act as defense molecule and intricate involvement in almost every function that a cell carries to sustain thrive exist proliferate and die. Disease and ailments are also by virtue of short-circuiting of these molecules caused by mutation or hostile condition. An understanding of pathophysiology of microbes within host and the unique proteins involved would open new pathway for global fight against these by targeted approach and structure based drug design and not by luck and serendipity. Mycobacterium tuberculosis is one such organism whose metabolic plasticity has tricked the scientific fraternity world over. With global efforts to target the survival salvage that these bacterium adopt to persist. The work embodied in the dissertation concerns with the two unique metabolic enzymes of glyoxylate pathway of Mycobacterium tuberculosis Isocitrate Lyase and Malate synthase. The endeavour of the project was to study the structure stability and functional aspects of these molecules and to account for various interactions and forces involved. The First Chapter Introduction is a bird‟s eye view of protein as biomolecules , their structure stability and folding, the misfolding , diseases, techniques and need to study these. The Second Chapter is review briefly presenting the problem, the culprit, the metabolic u-turn, survival salvage and odyssey to the literature of the two enzymes and their multiple roles. Third Chapter briefly describes the various materials used the methods undertaken and protocol followed. It outlines the experimental procedures undertaken to successfully carry out the studies. Fourth Chapter deals with the details of functional and structural properties of Isocitrate lyase of Mycobacterium tuberculosis and their modulation by divalent ions. Fifth and Six chapter has two interesting projects the first one incorporates Structural and Stability characteristics of Mycobacterium tuberculosis Malate synthase G and its comparison with E.coli homolog and the second project put forward the concept of existence of a functionally active dimer of Mycobacterium tuberculosis Malate synthase G. |
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4006582 bytes
application/pdf |
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| Language |
en
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| Relation |
CSIR-CDRI Thesis No. - K-108
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Isocitrate Lyase
Malate Synthase Mycobacterium tuberculosis |
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| Title |
Structural and Functional studies on Isocitrate Lyase and Malate Synthase from Mycobacterium tuberculosis
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Thesis
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