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SUMMARY:Sequential and Structural Determinants of Protein Aggregation - Dr
 . Natalia Sanchez de Groot\, Universitat Autònoma de Barcelona\, Spain
DTSTART:20100215T161500Z
DTEND:20100215T170000Z
UID:TALK23368@talks.cam.ac.uk
CONTACT:M. Madan Babu
DESCRIPTION:Protein aggregation is related with an increasing number of hu
 man disorders such as Alzheimer’s disease\, Parkinson disease or type II
  diabetes. Understanding the determinants that modulate the deposition pro
 cess is a necessary step to develop new strategies to tackle these debilit
 ating pathologies. Additionally\, the accumulation of heterologous protein
  as intracellular aggregates during recombinant expression represents one 
 of the main problems in down stream processing. Accordingly\, understandin
 g the factors behind the production of recombinant protein might lead to n
 ew avenues to increase the solubility and functionality of recombinant pro
 teins. During the development of the present research we have used a wide 
 range of techniques to analyse protein aggregation process in three differ
 ent frameworks: in vitro\, in vivo and in silico. The depositional propert
 ies of polypeptides differing in structure\, sequence\, and function were 
 studied. The data obtained reveal the importance of the intrinsic polypept
 ide chain properties to protein aggregation and reveal the general rules c
 ontrolling polypeptide deposition. This information permitted the developm
 ent of an algorithm able to locate key depositional regions and calculate 
 the global aggregation propensity of a protein starting from their amino a
 cid sequence. This tool can be used for the analysis of the aggregation pr
 operties of large protein sets as show here for cytosolic bacterial protei
 ns.
LOCATION:Level 4 Cell Biology Seminar Room\, MRC Laboratory of Molecular B
 iology\, Cambridge\, UK
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