| This session seeks submissions in the areas of experimental,
theoretical, and computational approaches to rational prediction,
design, and/or optimization of protein structure, stability, and
function in laboratory and processing settings relevant to
biopharmaceutical products in general. Studies may include structural
analysis and engineering of proteins, creation or optimization of
function, thermodynamics and dynamics of protein conformational
stability, issues in folding or misfolding, degradation via physical and
chemical routes, or related concerns in intracellular expression and
refolding, purification, and final product formulation. Preference will
be given to papers dealing with strategies that are relevant to
commercial and biological systems and also provide insights into the
molecular pathways or mechanisms controlling behavior. |
Structure and Aggregation in a Simple Helix-Forming Polymer
James Magee, Leo Lue and Robin Curtis, School of Chemical Engineering and Analytical Science, University of Manchester, PO Box 88, Sackville Street, Manchester M60 1QD, United Kingdom |
Smart Polymer Enhanced Protein Refolding: Molecular Dynamic Simulation and Experimental Validation
Diannan Lu1, Zheng Liu1 and Jianzhong Wu2, (1)Chemical Engineering, Tsinghua University, Beijing, China, (2)Chemical Engineering, University of California, Riverside, 3637 Canyon Crest Drive, Mailbox #516, Riverside, CA 92507 |
Computer Simulation of Protein Aggregation Kinetics Using an Intermediate Resolution Model
Erin M. Phelps and Carol K. Hall, Department of Chemical and Biomolecular Engineering, North Carolina State University, College of Engineering 1, Box 7905, 911 Partners Way, Raleigh, NC 27695 |
Structure, Stability and Formation of the Nucleus in Polyglutamine Aggregation
Allam S. Reddy1, Manan Chopra1, Nitin Rathore2 and Juan J. De Pablo1, (1)Department of Chemical and Biological Engineering, University of Wisconsin-Madison, 1415 Engineering Drive, Madison, WI 53706-1691, (2)University of Wisconsin Madison, 1415 Engineering Dr, Madison, WI 53706 |
Salt Effects on the Aggregation of Amyloid Fibril Forming Proteins
James M. Broering, Chemical & Biomolecular Engineering, Georgia Tech, 315 Ferst Dr, Atlanta, GA 30332-0363, Victor Yeh, School of Chemistry & Biochemistry, Georgia Institute of Technology, 315 Ferst Dr, Atlanta, GA 30332-0363 and Andreas S. Bommarius, Georgia Institute of Technology, School of Chemical Engineering, 315 Ferst Drive N.W., Parker H. Petit Biotechnology Institute, Room 3310, Atlanta, GA 30332-0363 |
Molecular Insights into Interactions between Misfolded Proteins and Application to Prion Transmission Barriers
Peter M. Tessier and Susan Lindquist, Whitehead Institute for Biomedical Research, 9 Cambridge Center, Cambridge, MA 02142 |
Protein Aggregation at Interfaces – Lipid Induced Amyloid-Beta Fibril Formation
Eva Y. Chi, Canay Ege, Shelli L. Frey and Ka Yee C. Lee, Department of Chemistry, The University of Chicago, 5735 S. Ellis Ave., Chicago, IL 60637 |
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