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Structural Engineering of the de novo Designed Protein Top7 as
a Scaffold for Antigen-binding


EMSL Project ID
19849

Abstract

Deployable biosensors for detecting environmental contaminants at the source require molecular sensing elements or affinity reagents that can survive the fluctuations in temperature and complex samples that are encountered in the field. All-atom molecular dynamics (MD) simulations will be performed for top7 variants - 5, 10 or 15 residue insertions at each of the six loop - in different solvents (water and methanol) and at different conditions of temperature and pH.

Project Details

Project type
Large-Scale EMSL Research
Start Date
2006-10-01
End Date
2009-09-30
Status
Closed

Team

Principal Investigator

Cheryl Baird
Institution
Pacific Northwest National Laboratory

Team Members

Curt Boschek
Institution
Pacific Northwest National Laboratory

David Apiyo
Institution
Pacific Northwest National Laboratory

Thereza Soares Da Silva
Institution
Universidade Federal de Pernambuco

T. Straatsma
Institution
Oak Ridge National Laboratory

Related Publications

Engineering an ultra-stable affinity reagent based on Top7 Curt B. Boschek1, David O. Apiyo1,3, Thereza A. Soares2, Heather E. Engelmann1, Noah B. Pefaur1,4, Tjerk P. Straatsma2 and Cheryl L. Baird1,5 1Cell Biology and Biochemistry Group, 2Computational Biology and Bioinformatics Group, Pacific Northwest National Laboratory, PO Box 999, MS K4-12, Richland, WA 99352, USA 3Present address: Beckman Coulter, Immunoassay Business Center, Chaska, MN 55318, USA 4Present address: Department of Protein Biochemistry, ZymoGenetics, Seattle, WA 98102, USA
Soares, T.A. ; Boschek, C. B. ; Apiyo, D. ; Baird, C.L. ; Straatsma, T.P. 2010. Molecular basis of the structural stability of a Top7-based scaffold under extreme pH and temperature conditions. J. Mol. Graph. and Mod., v. 28, p. 755-765.