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SUMMARY:Using Sequence Data to Probe the Determinants of Higher Order Stru
 cture in Fibrallar Collagens - Anna Puszkarska\, University of Cambridge
DTSTART:20180509T134000Z
DTEND:20180509T140000Z
UID:TALK101533@talks.cam.ac.uk
CONTACT:Lisa Masters
DESCRIPTION:The topology of connective tissues\, such as tendons\, skin\, 
 bones or cartilage is controlled to a large extent by the variety of assem
 blies formed by a specific class of proteins\, namely fibrillar collagens
 . Members of this group make up the most abundant proteins in our body\; t
 hese polymers and the higher-order structures that they form provide mecha
 nical support within every tissue in which they are present. Although\, fu
 ndamentally\, fibrillar collagen proteins exhibit high level of structura
 l and functional homology\, each collagen molecule has its own unique unde
 rlying composition\, and this composition is responsible for providing the
  specific designed features of each protein at the molecular level. Given
  the set of homologous sequences\, we build probabilistic models of collag
 en sequences to identify informative regions and correlations within and a
 mong polypeptide chains\; revealing which parts of the sequence confer spe
 cificity for each collagen chain\, making it unique and distinct from oth
 ers. Furthermore we probe which pairs of sequence positions depend on each
  other to obtain better understanding of the functionality of collagen mol
 ecules.
LOCATION:Department of Chemistry\, Cambridge\, Unilever lecture theatre
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