Browsing by Subject "Bacterial Proteins"
Now showing items 1-6 of 6
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DNA Repair Proteins in Mycobacteria and their Physiological Importance
(2018-03-09)DNA repair proteins in mycobacteria and their physiological importance Mycobacterium tuberculosis, the causative organism of tuberculosis, resides in the host macrophages where it is subjected to a plethora of stresses ... -
The Dynamics of Iron in Miniferritins : A Structure-Function Connection
(2017-11-23)The DNA binding proteins under starvation (Dps) from M. smegmatis are cage-like structures which internalize iron and bind DNA. They provide resistance to the cells from free radical damage, and physically protect the DNA ... -
Expanding The Horizon Of Mycobacterial Stress Response : Discovery Of A Second (P)PPGPP Synthetase In Mycobacterium Smegmatis
(2015-12-21)The stringent response is a highly conserved physiological response mounted by bacteria under stress (Ojha and Chatterji, 2001; Magnusson et al., 2005; Srivatsan and Wang, 2007; Potrykus and Cashel, 2008). Until recently, ... -
Regulation of the Principal Cell Division Protein FtsZ of Escherichia Coli by Antisense RNA and FtsH Protease
(2018-05-10)The PhD thesis is on the studsy of the influence of the ftsZ antisense RNA and FtsH protease on the synthesis and function of the Escherichia coli cytokinetic protein, FtsZ, which mediates septation during cell division. ... -
Structural and Related Studies on Mycobacterial Lectins
(2018-05-09)This thesis is concerned with the first ever X-ray crystallographic and complimentary solution studies on mycobacterial lectins. Lectins, described as multivalent carbohydrate binding proteins of non-immune origin, are ... -
Structural Studies on the Role of Hinge involved in Domain Swapping in Salmonella Typhimurium Stationary Phase Survival Protein (SurE) and Sesbania Mosaic Virus Coat Protein
(2018-05-09)A unique mechanism of protein oligomerization is domain swapping. It is a feature found in some proteins wherein a dimer or a higher oligomer is formed by the exchange of identical structural segments between protomers. ...