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
Released Data Link
Team
Principal Investigator
Team Members
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.