* Your assessment is very important for improving the workof artificial intelligence, which forms the content of this project
Download Proteins Behaving badly - The University of Oklahoma
Survey
Document related concepts
Signal transduction wikipedia , lookup
G protein–coupled receptor wikipedia , lookup
Protein (nutrient) wikipedia , lookup
Magnesium transporter wikipedia , lookup
List of types of proteins wikipedia , lookup
Protein domain wikipedia , lookup
Protein structure prediction wikipedia , lookup
Protein folding wikipedia , lookup
Protein phosphorylation wikipedia , lookup
Protein moonlighting wikipedia , lookup
Intrinsically disordered proteins wikipedia , lookup
Nuclear magnetic resonance spectroscopy of proteins wikipedia , lookup
Protein mass spectrometry wikipedia , lookup
Transcript
SCHOOL OF CHEMICAL, BIOLOGICAL & MATERIALS ENGINEERING And UNIVERSITY OF OKLAHOMA BIOENGINEERING CENTER The University of Oklahoma Norman, Oklahoma 2007 – 2008 Seminar Series CBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBME CBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBMECBME OUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOU BCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBCOUBC DR. REGINA MURPHY PROFESSOR DEPARTMENT OF CHEMICAL AND BIOLOGICAL ENGINEERING UNIVERSITY OF WISCONSIN, MADISON MADISON, WISCONSIN Will present a seminar on “PROTEINS BEHAVING BADLY: PROTEIN MISFOLDING AND AGGREGATION IN NEURODEGENERATIVE DISEASE” The spontaneous conversion of soluble proteins or protein fragments into insoluble aggregates with fibrillar morphology and a regular cross-b sheet structure is linked to a number of neurodegenerative diseases. These aggregates, called amyloid, are believed to be the root cause of disease pathology. Although it was once believed that the insoluble aggregates were the biologically active species, a growing body of data suggests that intermediates along the aggregation pathway, rather than the final product of aggregation, are responsible for the neuronal dysfunction and death observed in these diseases. Thus, the pathway and kinetics of aggregation of amyloidogenic proteins and peptides become biologically relevant. In this talk we will present ongoing research in two specific applications. First, we are examining the aggregation of beta-amyloid peptide, a protein fragment associated with Alzheimer's disease. We are particularly interested in the mechanism by which the protein transthyretin regulates beta-amyloid aggregation kinetics, because there is evidence in transgenic mice studies that transthyretin protects the mice from beta-amyloid toxicity. Second, we are developing methods to examine the role of expanded polyglutamine domains in aggregation of proteins associated with Huntington's and related diseases. We have begun a detailed examination of the role of polyglutamine length and position on protein stability, misfolding, and aggregation. Our hope is that these studies will contribute to establishing a physicochemical framework for understanding how, when, and why proteins misfold and aggregate into biological "bad actors", and for developing novel strategies for intervening in protein misfolding diseases. THURSDAY, MARCH 13, 2008 COOKIES AND COFFEE -- 2:15 P.M. SEMINAR -- 2:30 P.M. SARKEYS ENERGY CENTER, ROOM M-204 THIS IS A REQUIRED SEMINAR FOR CHE 5971