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UID:62@cds.iisc.ac.in
DTSTART;TZID=Asia/Kolkata:20240716T110000
DTEND;TZID=Asia/Kolkata:20240716T120000
DTSTAMP:20240708T063449Z
URL:https://cds.iisc.ac.in/events/ph-d-thesis-colloquium-102-cds-16-july-2
 024-structural-and-functional-studies-on-the-hypothetical-protein-ttha1873
 -from-thermus-thermophilus/
SUMMARY:Ph.D: Thesis Colloquium: 102 : CDS: 16\, July 2024 "Structural and 
 functional studies on the hypothetical protein TTHA1873 from Thermus therm
 ophilus"
DESCRIPTION:DEPARTMENT OF COMPUTATIONAL AND DATA SCIENCES\nPh.D. Thesis Col
 loquium\n\n\n\nSpeaker : Mr. Yuvaraj I\nS.R. Number : 06-18-01-10-12-13-1-
 10377\nTitle : "Structural and functional studies on the hypothetical prot
 ein TTHA1873 from Thermus thermophilus"\nResearch Supervisor : Prof. K. Se
 kar\nDate &amp\; Time : July 16\, 2024 (Tuesday)\, 11:00 AM\nVenue : # 102
  CDS Seminar Hall\n\n\n\nABSTRACT\n\nThis thesis reports a detailed study 
 on the structural and functional characterization of the hypothetical prot
 ein (TTHA1873) from Thermus thermophilus. In this study\, we characterized
  both the structure and function of TTHA1873. To elucidate the novel struc
 ture of this uncharacterized protein\, the study employed a heavy atom der
 ivative compound K 2 [HgI 4 ] to obtain an anomalous signal using home sou
 rce X-ray. The structural information obtained was then used to infer the 
 function of this protein. Biochemical experiments demonstrated that TTHA18
 73 acts as a nuclease\, indiscriminately cutting methylated and non-methyl
 ated DNA in divalent metal ions and relaxing plasmid DNA in the presence o
 f ATP. Its activity is inhibited by EDTA. Structural analysis identified f
 unctionally important residues\, and molecular dynamics simulations were c
 onducted to investigate the effects of mutating two critical residues on D
 NA binding.\n\nThe study explored the effects of high temperatures on this
  protein through molecular dynamics\, identifying temperature-sensitive re
 gions and providing insights into thermal denaturation. The use of heavy a
 tom compound K 2 [HgI 4 ] to obtain phases has been previously reported in
  the literature. Still\, the protocols used to solve the three-dimensional
  structure of this protein may be particularly useful in challenging cases
  where molecular replacement is ineffective or when no similar structures 
 are available in the Protein Data Bank (PDB)\, without relying on a synchr
 otron source.\n\n\n\nALL ARE WELCOME
CATEGORIES:Events,Ph.D. Thesis Colloquium
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