Abstract

Aim 1. Develop and validate novel methods and technologies for the reliable expression of IMPs. Secondary goal is to reduce the cost of IMP expression. a. Cell free expression - conduct a systematic expression survey with a representative number of IMPs and then develop novel technologies to increase the reliability of the system. b. Baculovirus expression - conduct a systematic expression survey with a representative number of IMPs in different insect cell types. Develop novel methods and technologies to reduce the complexity of the processes, increase reliability of the technology using novel flow cytometry technologies, and lower the cost of expression through miniaturization. c. Mammalian expression - conduct a systematic expression survey with a representative number of IMPs in different mammalian cell types and analyze gene expression profiles during over-expression. Develop novel methods and technologies to reduce the complexity of the processes, increase reliability of the technology using novel flow cytometry technologies, and lower the cost of expression through miniaturization.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Specialized Center (P50)
Project #
5P50GM073197-02
Application #
7114417
Study Section
Special Emphasis Panel (ZGM1)
Project Start
Project End
Budget Start
2005-08-01
Budget End
2006-07-31
Support Year
2
Fiscal Year
2005
Total Cost
$861,807
Indirect Cost

  Institution

Name
Scripps Research Institute
Department
Type
DUNS #
781613492
City
La Jolla
State
CA
Country
United States
Zip Code
92037

  Publications

Ishchenko, Andrii; Peng, Lingling; Zinovev, Egor et al. (2017) Chemically Stable Lipids for Membrane Protein Crystallization. Cryst Growth Des 17:3502-3511
Lamichhane, Rajan; Liu, Jeffrey J; Pauszek 3rd, Raymond F et al. (2017) Fluorophore Labeling, Nanodisc Reconstitution and Single-molecule Observation of a G Protein-coupled Receptor. Bio Protoc 7:
Eddy, Matthew T; Didenko, Tatiana; Stevens, Raymond C et al. (2016) ?2-Adrenergic Receptor Conformational Response to Fusion Protein in the Third Intracellular Loop. Structure 24:2190-2197
Rowe, Timothy B; Luo, Zhe-Xi; Ketcham, Richard A et al. (2016) X-ray computed tomography datasets for forensic analysis of vertebrate fossils. Sci Data 3:160040
Bennett, Brad C; Purdy, Michael D; Baker, Kent A et al. (2016) An electrostatic mechanism for Ca(2+)-mediated regulation of gap junction channels. Nat Commun 7:8770
Didenko, Tatiana; Proudfoot, Andrew; Dutta, Samit Kumar et al. (2015) Non-Uniform Sampling and J-UNIO Automation for Efficient Protein NMR Structure Determination. Chemistry 21:12363-9
Horst, Reto; Wüthrich, Kurt (2015) Micro-scale NMR Experiments for Monitoring the Optimization of Membrane Protein Solutions for Structural Biology. Bio Protoc 5:
O'Connor, Casey; White, Kate L; Doncescu, Nathalie et al. (2015) NMR structure and dynamics of the agonist dynorphin peptide bound to the human kappa opioid receptor. Proc Natl Acad Sci U S A 112:11852-7
Lamichhane, Rajan; Liu, Jeffrey J; Pljevaljcic, Goran et al. (2015) Single-molecule view of basal activity and activation mechanisms of the G protein-coupled receptor ?2AR. Proc Natl Acad Sci U S A 112:14254-9
Moeller, Arne; Lee, Sung Chang; Tao, Houchao et al. (2015) Distinct conformational spectrum of homologous multidrug ABC transporters. Structure 23:450-460

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