This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. The COBRE Core B Protein Production Core Laboratory is hosted within The University of Kansas Higuchi Bioscience Center and is housed in the Shankel Structural Biology Center. The lab focuses on the cloning, expression and purification of prokaryotic and eukaryotic proteins for researchers who need to obtain proteins for their research, which adds technical support to individual research groups. The Core works closely with the Bio-NMR Core Laboratory, the Protein Structure Core Laboratory, and the High Throughput Screening Laboratory. The Core B laboratory provides a one-stop menu of services to investigators, including protocol development;cloning;mutagenesis;expression system development or improvement;large or small scale protein expression and/or purification;Biacore binding studies;and technical training for researchers in any of these areas. The staff can perform protein expression in either bacterial or insect cell systems. The core laboratory possesses the equipment and personnel required for overexpression and purification of properly folded and functional proteins in quantities sufficient for a variety of applications, including functional and binding studies. The major equipment in the facility includes: Shaker-incubators;Automated fermentation (1-10 L scale);AKTAXpress, AKTA Purifier system and FPLC system;Constant Systems Hydraulic Cell Disruptor, and a Biacore 3000 Surface Plasma Resonance system. In addition, the laboratory provides advice on the generation and analysis of proteins depending on their physicochemical properties and the needs of the investigator. The staff consists of a Director and one full time technician.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Exploratory Grants (P20)
Project #
5P20RR017708-09
Application #
8359658
Study Section
National Center for Research Resources Initial Review Group (RIRG)
Project Start
2011-04-01
Project End
2012-03-31
Budget Start
2011-04-01
Budget End
2012-03-31
Support Year
9
Fiscal Year
2011
Total Cost
$185,660
Indirect Cost
Name
University of Kansas Lawrence
Department
Pharmacology
Type
Schools of Pharmacy
DUNS #
076248616
City
Lawrence
State
KS
Country
United States
Zip Code
66045
Garabedian, Alyssa; Baird, Matthew A; Porter, Jacob et al. (2018) Linear and Differential Ion Mobility Separations of Middle-Down Proteoforms. Anal Chem 90:2918-2925
Jeanne Dit Fouque, Kevin; Garabedian, Alyssa; Porter, Jacob et al. (2017) Fast and Effective Ion Mobility-Mass Spectrometry Separation of d-Amino-Acid-Containing Peptides. Anal Chem 89:11787-11794
Alaofi, Ahmed; Farokhi, Elinaz; Prasasty, Vivitri D et al. (2017) Probing the interaction between cHAVc3 peptide and the EC1 domain of E-cadherin using NMR and molecular dynamics simulations. J Biomol Struct Dyn 35:92-104
Pang, Xiao-Yan; Wang, Suya; Jurczak, Michael J et al. (2017) Retinol saturase modulates lipid metabolism and the production of reactive oxygen species. Arch Biochem Biophys 633:93-102
McNiff, Michaela L; Chadwick, Jennifer S (2017) Metal-bound claMP Tag inhibits proteolytic cleavage. Protein Eng Des Sel 30:467-475
Johnson, Troy A; Mcleod, Matthew J; Holyoak, Todd (2016) Utilization of Substrate Intrinsic Binding Energy for Conformational Change and Catalytic Function in Phosphoenolpyruvate Carboxykinase. Biochemistry 55:575-87
Tucker, Jenifer K; McNiff, Michaela L; Ulapane, Sasanka B et al. (2016) Mechanistic investigations of matrix metalloproteinase-8 inhibition by metal abstraction peptide. Biointerphases 11:021006
Yadav, Rahul; Vattepu, Ravi; Beck, Moriah R (2016) Phosphoinositide Binding Inhibits Actin Crosslinking and Polymerization by Palladin. J Mol Biol 428:4031-4047
Gurung, Ritu; Yadav, Rahul; Brungardt, Joseph G et al. (2016) Actin polymerization is stimulated by actin cross-linking protein palladin. Biochem J 473:383-96
Budiardjo, S Jimmy; Licknack, Timothy J; Cory, Michael B et al. (2016) Full and Partial Agonism of a Designed Enzyme Switch. ACS Synth Biol 5:1475-1484

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