The Biophysics Resource (BR) is managed and operated by the Structural Biophysics Laboratory. BR provides expert staff to assist users in the design of experiments and operation of advanced biophysical chemistry technologies such as circular dichroism spectroscopy, LC/MS and LC/MS/MS spectrometry(including high-resolution option), steady-state fluorescence spectroscopy, isothermal titration calorimetry, differential scanning calorimetry, dynamic and static light scattering, microscale thermophoresis for characterization of biomacromolecules and/or their complexes. The BR provides much more than simple instrument availability by training in the use of instruments, maintenance and upgrades of instrumentation, and consultation/collaboration on experimental design and sophisticated analysis of biophysical experiments. The BR assists researchers from other Institutes on a time-available basis. The BR is the only place at CCR providing service-oriented access to such technologies as titration and scanning calorimetry, circular dichroism, microscale thermophoresis. Majority of BR technologies, even mass-spectroscopy, operate in walk-up mode and experiments are run by users after necessary training. It allows minimization of the time interval for complex technologies between project initialization and final result from days and hours down to minutes, if necessary.

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Scientific Cores Intramural Research (ZIC)
Project #
1ZICBC010965-06
Application #
8763739
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
6
Fiscal Year
2013
Total Cost
$464,878
Indirect Cost
Name
National Cancer Institute Division of Basic Sciences
Department
Type
DUNS #
City
State
Country
Zip Code
Tewary, Poonam; de la Rosa, Gonzalo; Sharma, Neeraj et al. (2013) β-Defensin 2 and 3 promote the uptake of self or CpG DNA, enhance IFN-α production by human plasmacytoid dendritic cells, and promote inflammation. J Immunol 191:865-74
Liu, Shan; Chen, Yinghua; Li, Jess et al. (2012) Promiscuous interactions of gp78 E3 ligase CUE domain with polyubiquitin chains. Structure 20:2138-50
Timofeeva, Olga A; Chasovskikh, Sergey; Lonskaya, Irina et al. (2012) Mechanisms of unphosphorylated STAT3 transcription factor binding to DNA. J Biol Chem 287:14192-200
Tarasov, Sergey G; Gaponenko, Vadim; Howard, O M Zack et al. (2011) Structural plasticity of a transmembrane peptide allows self-assembly into biologically active nanoparticles. Proc Natl Acad Sci U S A 108:9798-803
Tu, Chao; Zhou, Xiaomei; Tarasov, Sergey G et al. (2011) The Era GTPase recognizes the GAUCACCUCC sequence and binds helix 45 near the 3' end of 16S rRNA. Proc Natl Acad Sci U S A 108:10156-61
Johannessen, Liv; Remsberg, Jarrett; Gaponenko, Vadim et al. (2011) Peptide structure stabilization by membrane anchoring and its general applicability to the development of potent cell-permeable inhibitors. Chembiochem 12:914-21
Stagno, Jason R; Altieri, Amanda S; Bubunenko, Mikhail et al. (2011) Structural basis for RNA recognition by NusB and NusE in the initiation of transcription antitermination. Nucleic Acids Res 39:7803-15
Li, Chong; Pazgier, Marzena; Li, Jing et al. (2010) Limitations of peptide retro-inverso isomerization in molecular mimicry. J Biol Chem 285:19572-81
Pazgier, Marzena; Liu, Min; Zou, Guozhang et al. (2009) Structural basis for high-affinity peptide inhibition of p53 interactions with MDM2 and MDMX. Proc Natl Acad Sci U S A 106:4665-70
Das, Ranabir; Mariano, Jennifer; Tsai, Yien Che et al. (2009) Allosteric activation of E2-RING finger-mediated ubiquitylation by a structurally defined specific E2-binding region of gp78. Mol Cell 34:674-85