The mission ofthe COBRE-PSF Biomolecular NMR (BNMR) Core Lab (Core D) is to provide COBRE and other researchers with a full range of capabilities and services in high-field protein NMR including 1) consultation in experiment design and data acquisition, processing and interpretation, 2) training in instrument use, 3) access to instruments for qualified users, and 4) custom service in data acquisition for pilot, structural, dynamics and molecular interaction studies. The COBRE-PSF BNMR Core Lab was established in May 2008 at the start of Phase-ll of COBRE-PSF. A Lab Director experienced in protein NMR spectroscopy. Dr. Asokan Anbanadam, was hired in fall 2008 to operate the Lab, maintain the instruments and software, and provide training as well as services in protein NMR. The BNMR Lab has two major NMR instruments: an 800 MHz with a cryoprobe and a 600 MHz with room temperature triple-resonance probe, a multi heteronuclear probe and an automated sample changer. Since fall 2008 the BNMR Core Lab has served investigators from 28 different research groups located at nine different universities and institutes from around Kansas. During Phase III ofthe COBRE program the BNMR core will continue to provide access to state-of-the-art facilities and services to a growing range of COBRE and other investigators who appreciate the power that NMR can bring to their research on proteins. By growing its client base on top of a base of financial support promised by The University of Kansas, the COBRE-PSF BNMR Core Lab will become sustainable into the future.

Public Health Relevance

This Core Lab maintains two state-of-the-art Nuclear Magnetic Resonance (NMR) spectrometers dedicated to studies of proteins in soluition. The Core Lab also provides advice, training and/or services in experiment design, data collection and data interpretation for COBRE scientists and others on a fee-for-service basis

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Center Core Grants (P30)
Project #
1P30GM110761-01
Application #
8735422
Study Section
Special Emphasis Panel (ZGM1-TWD-C (C3))
Project Start
Project End
Budget Start
2014-08-01
Budget End
2015-06-30
Support Year
1
Fiscal Year
2014
Total Cost
$225,000
Indirect Cost
$75,000
Name
University of Kansas Lawrence
Department
Type
DUNS #
076248616
City
Lawrence
State
KS
Country
United States
Zip Code
66045
Wahome, Newton; Sully, Erin; Singer, Christopher et al. (2016) Novel Ricin Subunit Antigens With Enhanced Capacity to Elicit Toxin-Neutralizing Antibody Responses in Mice. J Pharm Sci 105:1603-13
Weerawarna, Pathum M; Kim, Yunjeong; Galasiti Kankanamalage, Anushka C et al. (2016) Structure-based design and synthesis of triazole-based macrocyclic inhibitors of norovirus protease: Structural, biochemical, spectroscopic, and antiviral studies. Eur J Med Chem 119:300-18
Wahome, Newton; Cooper, Anne; Thapa, Prem et al. (2016) Production of Well-Characterized Virus-like Particles in an Escherichia coli-Based Expression Platform for Preclinical Vaccine Assessments. Methods Mol Biol 1404:437-57
Jia, Kaimin; Cao, Ruikai; Hua, Duy H et al. (2016) Study of Class I and Class III Polyhydroxyalkanoate (PHA) Synthases with Substrates Containing a Modified Side Chain. Biomacromolecules 17:1477-85
McShan, Andrew C; Anbanandam, Asokan; Patnaik, Sikta et al. (2016) Characterization of the Binding of Hydroxyindole, Indoleacetic acid, and Morpholinoaniline to the Salmonella Type III Secretion System Proteins SipD and SipB. ChemMedChem 11:963-71
Gowthaman, Ragul; Miller, Sven A; Rogers, Steven et al. (2016) DARC: Mapping Surface Topography by Ray-Casting for Effective Virtual Screening at Protein Interaction Sites. J Med Chem 59:4152-70
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
Tifrea, Delia F; Barta, Michael L; Pal, Sukumar et al. (2016) Computational modeling of TC0583 as a putative component of the Chlamydia muridarum V-type ATP synthase complex and assessment of its protective capabilities as a vaccine antigen. Microbes Infect 18:245-53
Kaur, Kawaljit; Chatterjee, Srirupa; De Guzman, Roberto N (2016) Characterization of the Shigella and Salmonella Type III Secretion System Tip-Translocon Protein-Protein Interaction by Paramagnetic Relaxation Enhancement. Chembiochem 17:745-52
O'Neil, Pierce; Lovell, Scott; Mehzabeen, Nurjahan et al. (2016) Crystal structure of histone-like protein from Streptococcus mutans refined to 1.9 Å resolution. Acta Crystallogr F Struct Biol Commun 72:257-62

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