BEGIN:VCALENDAR
VERSION:2.0
PRODID:-//CERN//INDICO//EN
BEGIN:VEVENT
SUMMARY:Reconciling Synchrotron SAXS Data with NMR Data for a Two-Domain P
 rotein
DTSTART;VALUE=DATE-TIME:20141120T063000Z
DTEND;VALUE=DATE-TIME:20141120T080000Z
DTSTAMP;VALUE=DATE-TIME:20260712T184758Z
UID:indico-contribution-738@events01.synchrotron.org.au
DESCRIPTION:Speakers: Geoffrey Jameson (Massey University)\nA preliminary 
 structure of the protein Yih1 (Yeast impact homologue 1)\, a protein of pa
 rtially characterised function\, has been obtained by multi-dimensional NM
 R methods. The ~300-residue protein has two distinct domains of approximat
 ely 120 and 160 residues with an approximately 20-residue linker. However\
 , no NOEs could be found involving contacts between the two domains. Solut
 ion-state SAXS data were recorded at the Australian Synchrotron. The struc
 ture is clearly monomeric. The NMR structure of one domain was then transl
 ated and rotated relative to the other domain until a remarkably good fit 
 to the distinctive SAXS data was obtained. The interaction between the two
  domains was then\, and only then\, inspected and found to involve a fairl
 y loose and not implausible association via a small hydrophobic patch and 
 several potential salt bridges. Residual dipolar coupling measurements are
  in progress to determine alignment vectors of the two domains\, and confi
 rm\, or otherwise\, the accuracy of the SAXS model of domain association. 
      \n\nCambiaghi TD\, Pereira CM\, Shanmugam R\, Bolech M\, Wek RC\, Sat
 tlegger E\, Castilho BA. 2014.\nEvolutionarily conserved IMPACT impairs va
 rious stress responses that require GCN1 for activating the eIF2 kinase GC
 N2. Biochem Biophys Res Commun 443: 592-597 (doi: 10.1016/j.bbrc.2013.12.0
 21).\n\nhttps://events01.synchrotron.org.au/event/3/contributions/738/
LOCATION: NCSS Exhibition Area
URL:https://events01.synchrotron.org.au/event/3/contributions/738/
END:VEVENT
END:VCALENDAR