Abstract

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 aim of the Biomolecular NMR Laboratory (CORE D) is to assist investigators in getting fast and high quality results from the 800 and 600 MHz NMR instruments available at The University of Kansas. These instruments are used mostly for biomolecular NMR research in understanding structure, function and dynamics of proteins and associated complexes. The COBRE in Protein Structure and Function has hired a biomolecular NMR specialist, Asokan Anbanandam, to assist investigators in support of their investigations of protein structure, function and dynamics. Anbanandam is responsible for day-to-day operation, maintenance, user training, and hardware and software upgrades of the 800 and 600 MHz NMR instruments. Anbanandam also aids local and remote users in NMR data acquisition, processing and analysis.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Exploratory Grants (P20)
Project #
5P20RR017708-09
Application #
8359659
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
$104,172
Indirect Cost

  Institution

Name
University of Kansas Lawrence
Department
Pharmacology
Type
Schools of Pharmacy
DUNS #
076248616
City
Lawrence
State
KS
Country
United States
Zip Code
66045

  Publications

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
McNiff, M L; Haynes, E P; Dixit, N et al. (2016) Thioredoxin fusion construct enables high-yield production of soluble, active matrix metalloproteinase-8 (MMP-8) in Escherichia coli. Protein Expr Purif 122:64-71
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

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