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UID:80@cds.iisc.ac.in
DTSTART;TZID=Asia/Kolkata:20241114T110000
DTEND;TZID=Asia/Kolkata:20241114T120000
DTSTAMP:20241105T003551Z
URL:https://cds.iisc.ac.in/events/ph-d-thesis-defense-102-cds-seminar-hall
 -14-november-2024-structural-and-functional-studies-on-the-hypothetical-pr
 otein-ttha1873-from-thermus-thermophilus/
SUMMARY:Ph.D. Thesis Defense: #102: CDS Seminar Hall: 14\, November 2024 "S
 tructural and functional studies on the hypothetical protein TTHA1873 from
  Thermus thermophilus"
DESCRIPTION:DEPARTMENT OF COMPUTATIONAL AND DATA SCIENCES\nPh.D. Thesis Def
 ense\n\n\n\nSpeaker : Mr. Yuvaraj I\nS.R. Number : 06-18-01-10-12-13-1-103
 77\nTitle : "Structural and functional studies on the hypothetical protein
  TTHA1873 from Thermus thermophilus"\nResearch Supervisor : Prof. K. Sekar
 \nDate &amp\; Time : November 14\, 2024 (Thursday)\, 11:00 AM\nVenue : # 1
 02 CDS Seminar Hall\n\n\n\nABSTRACT\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. The study explored the effects of high temperatures on this pr
 otein through molecular dynamics\, identifying temperature-sensitive regio
 ns and providing insights into thermal denaturation. The use of heavy atom
  compound K 2 [HgI 4 ] to obtain phases has been previously reported in th
 e literature. Still\, the protocols used to solve the three-dimensional st
 ructure of this protein may be particularly useful in challenging cases wh
 ere molecular replacement is ineffective or when no similar structures are
  available in the Protein Data Bank (PDB)\, without relying on a synchrotr
 on source.\n\n\n\nALL ARE WELCOME
CATEGORIES:Events,Thesis Defense
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