BEGIN:VCALENDAR VERSION:2.0 METHOD:PUBLISH PRODID:-//Missouri State University/Calendar of Events//EN CALSCALE:GREGORIAN X-WR-TIMEZONE:America/Chicago BEGIN:VTIMEZONE TZID:America/Chicago BEGIN:DAYLIGHT TZOFFSETFROM:-0600 TZOFFSETTO:-0500 DTSTART:20070311T020000 RRULE:FREQ=YEARLY;BYMONTH=3;BYDAY=2SU TZNAME:CDT END:DAYLIGHT BEGIN:STANDARD TZOFFSETFROM:-0500 TZOFFSETTO:-0600 DTSTART:20071104T020000 RRULE:FREQ=YEARLY;BYMONTH=11;BYDAY=1SU TZNAME:CST END:STANDARD END:VTIMEZONE BEGIN:VEVENT UID:58a93243-4007-4d64-bd26-52bc8878bacf.180987@calendar.missouristate.edu CREATED:20170710T190742Z LAST-MODIFIED:20170710T190742Z LOCATION:Kemper Hall 101M SUMMARY:Thesis Defense: Shah Alam Limon\, Physics\, Astronomy & Materials Science DESCRIPTION:STUDY OF IRON ION TRANSIT THROUGH\n\n\nTHREE-FOLD CHANNEL OF F ERRITIN CAGE\n\n\nFerritin is an iron-storage protein with an ability to uptake\, mineralize and release iron ions in a controllable manner. Under standing of the detailed molecular functioning of ferritin is required fo r rational design of biomimetic conjugate nano-biosystems containing ferr itin-like constituents. In this work\, ferritin was investigated both num erically by all-atom molecular dynamics (MD) simulations using the GROMAC S tool\, and experimentally by Raman spectroscopy. Molecular dynamic simu lations of a model system comprising iron ions (Fe2+) and a ferritin trim er expressing a three-fold channel responsible for the ion transport\, ha ve revealed a quick entering of ions in the channel. The transit was foun d to be driven by both electrostatic charge of ferritin\, and interaction between the ions. Exit (expulsion) of an iron ion from the channel was o bserved at a condition that at least one more ion is present in the chann el. Otherwise\, a single ion may remain in the channel for a long time wi thout exiting. Raman characterization of an iron-loaded ferritin solution revealed pronounced bands attributable to iron\, as expected. The study of molecular mechanisms involved in the iron ion transit elucidates the p athways of iron uptake and release in ferritin. X-ALT-DESC;FMTTYPE=text/html:<html><head><title></title></head><body><p cl ass="MsoNormal" align="center"><span>STUDY OF IRON ION TRANSIT THROUGH<o: p></o:p></span></p>\n<p class="MsoNormal" align="center"><span>THREE-FOLD CHANNEL OF FERRITIN CAGE</span><span><o:p></o:p></span></p>\n<p class="M soNormal" align="center">Ferritin is an iron-storage protein with an abil ity to uptake\, mineralize and release iron ions in a controllable manner . Understanding of the detailed molecular functioning of ferritin is requ ired for rational design of biomimetic conjugate nano-biosystems containi ng ferritin-like constituents. In this work\, ferritin was investigated b oth numerically by all-atom molecular dynamics (MD) simulations using the GROMACS tool\, and experimentally by Raman spectroscopy. Molecular dynam ic simulations of a model system comprising iron ions (Fe<sup>2+</sup>) a nd a ferritin trimer expressing a three-fold channel responsible for the ion transport\, have revealed a quick entering of ions in the channel. Th e transit was found to be driven by both electrostatic charge of ferritin \, and interaction between the ions. Exit (expulsion) of an iron ion from the channel was observed at a condition that at least one more ion is pr esent in the channel. Otherwise\, a single ion may remain in the channel for a long time without exiting. Raman characterization of an iron-loaded ferritin solution revealed pronounced bands attributable to iron\, as ex pected. The study of molecular mechanisms involved in the iron ion transi t elucidates the pathways of iron uptake and release in ferritin.</p></bo dy></html> DTSTART;TZID=America/Chicago:20170714T160000 DTEND;TZID=America/Chicago:20170714T173000 SEQUENCE:0 URL:https://www.facebook.com/MSUPAMS2/ CATEGORIES:Current Students,Faculty,Staff END:VEVENT END:VCALENDAR