BEGIN:VCALENDAR
VERSION:2.0
PRODID:-//Talks.cam//talks.cam.ac.uk//
X-WR-CALNAME:Talks.cam
BEGIN:VEVENT
SUMMARY:Non-covalent Peptide Assembly: The latest Results - Mike Bowers\, 
 UC Santa Barbara
DTSTART:20151210T160000Z
DTEND:20151210T170000Z
UID:TALK62843@talks.cam.ac.uk
CONTACT:Jerome Charmet
DESCRIPTION:Non-covalent interactions precede almost all important biologi
 cal functions.  This is particularly so for peptides and proteins where th
 ey often assemble into myriad structures before they reach their active st
 ate.  There is also a down side to such assembly as exemplified by the man
 y amyloid systems that occur and provide the basis for many devastating di
 seases such as Alzheimer’s Disease\, Parkinson’s Disease\, Type 2 Diab
 etes and many more.  These can occur for systems as small as amino acids (
 phenylketonuria) or proteins of many hundreds of amino acids (taupathies).
   As a consequence it is of prime importance to understand the factors tha
 t drive these systems to self assemble so that effective therapeutic strat
 egies and agents can be designed and tested.  Here we will introduce the p
 roblem\, why it is so hard to study\, briefly describe the methods we use 
 to attack it and give our latest results.  We will demonstrate that ultra 
 soft ion mobility methods\, especially when coupled to mass spectrometry\,
  high level modeling and most recently to spectroscopy offer hope in under
 standing the size and conformation specific growth of amyloid systems\, wh
 ile other spectroscopies are ineffective.  We will focus in this talk on t
 he basic peptide assembly mechanism rather than directly on disease\, alth
 ough that will also play a part.
LOCATION:Department of Chemistry\, Cambridge\, Unilever lecture theatre
END:VEVENT
END:VCALENDAR