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http://psf.cobre.ku.edu/cores/bnmrl/about
NMR Laboratory maintains two high field NMR spectrometers in support of structural and dynamics studies of biomolecules. Its capabilities include determining high resolution structures, biological macromolecules, elucidation and structural mapping of protein-protein, protein-nucleic acid, protein-peptide, protein-drug interactions, and studies of dynamics of proteins and their complexes in solution. Laboratory staff provide advice,consultation, training,assistance and complete structure elucidation services.Staff is responsible for maintenance, upgrades, implementation of new NMR pulse sequences, and assisting local and remote users with technical problems.Equipped with Bruker Avance 800 MHz NMR instrument fitted with TCI cryoprobe and Bruker Avance III 600 MHz with variety of probes.
Proper citation: Kansas University Lawrence Biomolecular NMR Laboratory Core Facility (RRID:SCR_018671) Copy
Core provides expertise, services, education, and instrumentation to enhance biomedical research through LC-MS/MS-based proteomics. Services are offered for protein identification; characterization of post-translational modifications; and quantitative proteomics to identify differentially expressed/degraded proteins, regulated sites of post-translational modification, protein-protein interactions, and protein targets of drugs identified in phenotypic screens. Analyses include sample preparation, LC-MS/MS, database searching, generation of reports, and assistance with data interpretation. Faculty and staff assist with experimental design and development/optimization of customized methodology for analysis of post-translationally modified peptides (e.g. phosphorylation and O-GlcNAc modification, N- and O-linked glycosylation, Cys modifications including S-glutathionylation, and glycation of Lys and Arg). Quantitative approaches including metabolic labeling (SILAC), isobaric tagging (iTRAQ/TMT), and label free proteomics (LFQ) are performed on Orbitrap Elite or Orbitrap Fusion Lumos Mass Spectrometers. Developes methodology to identify alterations in post-translational modifications that impact signal transduction, transcription, translation, and response to therapeutics with goal of enabling investigators to discover molecular mechanisms underlying disease progression and therapeutic response.
Proper citation: South Carolina Medical University Mass Spectrometry Core Facility (RRID:SCR_017959) Copy
https://vbrn.org/proteomics-services/
Provides central resource of mass spectrometry based proteomics technologies to identify, characterize and quantify target proteins in various biological and biomedical samples. Provides mass spectrometry expertise for analyzing proteins and peptides for proteomics studies, support for data analysis from proteomics measurements, training in proteomics methods, and experimental design.
Proper citation: Vermont University Proteomics Core Facility (RRID:SCR_018667) Copy
Core provides physicochemical characterization of nanoscale entities. Offers characterization of several classes of nanomaterials:Polymer conjugates,Polymeric micelles,Liposomes,Nanogels,Polyion complexes of small drugs and biomacromolecules (proteins, DNA, and RNA),Inorganic/metal nanoparticles,Bio-derived nanoparticles such as exosomes with protein and nucleic acid cargo.
Proper citation: North Carolina University at Chapel Hill Nanomedicines Characterization Core Facility (RRID:SCR_017951) Copy
Core provides analytical redox biochemistry methods and mentoring support for COBRE junior faculty with goal to advance their research endeavors, publications and fundability. Specific aims are:Provide ROS /RNS identification and quantification, Perform quantitative analysis of ROS/RNS. Provides expertise and technology for in depth biochemical analysis of thiol-centered enzyme activities and define protein:protein interactions.
Proper citation: South Carolina Medical University Analytical Redox Biology Core Facility (RRID:SCR_017955) Copy
https://www.waksman.rutgers.edu/fermentation
Provides fermentation services. Produces range of bulk biologics including antimicrobials, cosmetic substrates, flavors/fragrances, biopesticides/bioherbicides and plasmid derived proteins, enzymes, growth factors and diagnostics. Exceptions for pathogenic or opportunistic organisms and mammalian and insect cell lines. Includes Material Preparation Laboratory,Fermentation In-Process/Computer Control,Product Recovery and Analytical Services.
Proper citation: Rutgers Waksman Institute of Microbiology Cell and Cell Products Fermentation Core Facility (RRID:SCR_018676) Copy
http://cobre.pbrc.edu/cores/genomics/
Provides services which include Sanger and next-generation DNA sequencing,DNA fragment analysis,qualitative and quantitative analysis of DNA, protein, and RNA samples, quantitative PCR, microarray RNA labeling, hybridization, and scanning robotics,bioinformatics.Individual and small group training and consultation services are offered for sequence analysis, real-time PCR, next-generation sequencing and microarray analysis.
Proper citation: Louisiana State University Pennington Biomedical Research Center Genomics Core Facility (RRID:SCR_018675) Copy
https://github.com/Wssduer/GraphRBF
Software tool as protein-protein/nucleic acid interaction site prediction model built by enhanced graph neural networks and prioritized radial basis function neural networks. Protein-protein and protein-nucleic acid binding site prediction via interpretable hierarchical geometric deep learning.
Proper citation: GraphRBF (RRID:SCR_025652) Copy
http://www.jhugicc.org/GIConteCenter/pages/cores/proteomicsCore.html
Core facility that uses mass spectrometry coupled to one (1D) and two (2D) dimensional separations by column chromatography or gel electrophoresis to identify, quantify or characterize proteins and their post-translational modifications, that are expressed in well characterized protein fractions from the small intestine, colon, kidney, liver and pancreas. Techniques such as difference gel electrophoresis (DIGE), isobaric tag for relative and absolute quantitation (iTRAQ), tandem mass tags (TMT) and stable isotope labeling of amino acids in cell culture (SILAC) as well as non-labeling methods (MudPIT, multi-dimensional protein identification technology) are available for quantifying relative differences in protein expression and post-translational modifications, such as acetylation, glycosylation, phosphorylation, nitrosation, ubiquitination and novel cleavage sites.
Proper citation: Hopkins Conte Digestive Diseases Basic and Translational Research Core Center Proteomics Core (RRID:SCR_015597) Copy
https://www.dbi.udel.edu/resources-and-facilities/protein-characterization
Facility consists of a Beckman Coulter ProteomeLab XL-I analytical ultracentrifuge is configured with a scanning UV/Vis detection system and Rayleigh Interference Optics. Used to characterize variety of biophysical properties of macromolecules such as molecular weight, sedimentation coefficient, diffusion coefficient, equilibrium constant and stoichiometry. Can assess sample heterogeneity (aggregation and purity), molecular conformation (folded or unfolded), composition (assembled or unassembled) and thermodynamic properties of interacting systems. Provides spectrum of data for protein characterization in solution.
Proper citation: Delaware Biotechnology Institute Protein Characterization Core Facility (RRID:SCR_017746) Copy
https://www.usd.edu/medicine/basic-biomedical-sciences/proteomics-core
Core provides proteomics services to researchers from South Dakota and the surrounding region to rapidly analyze and identify protein expression patterns in their experimental systems.Develops experimental design, protocols, data analysis and interpretation.Provides consulting and advice in grant proposal, as well as data preparation to be submitted to proteomics journal according to requirements.Offers training in use of common equipment such as scanner, spot cutter, imaging software, technique and protocol issues, and sample preparation.
Proper citation: South Dakota University SD BRIN Proteomics Core Facility (RRID:SCR_017743) Copy
https://www.cimr.cam.ac.uk/about/facilities/bioinformatics
Core provides biological data handling and analysis in differential expression analysis, next generation sequencing, networks, protein architecture, and motif searching for in house researchers.
Proper citation: Cambridge Institute for Medical Research Bioinformatics Core Facility (RRID:SCR_017186) Copy
http://www.columbia.edu/cu/biology/resources/proteomics/
Core provides identification of proteins and metabolites with differential quantitative expression in cells, tissues or in protein affinity purifications. Particular emphasis is on quantitative analysis of posttranslational modifications such as phosphorylation.
Proper citation: Columbia University Quantitative Proteomics and Metabolomics Core Facility (RRID:SCR_017747) Copy
http://www.uvm.edu/sbb/cxx/cxx.html
Core for high resolution structural biology at the University of Vermont. X-ray crystallography allows biological and biomedical researchers to visualize proteins, RNA, DNA and their complexes at atomic resolution. The molecular details of specimens as small as DNA binding domains and as large as the ribosome have been elucidated via this powerful method. The CXX provides resources for all stages of macromolecular structure determination.
Proper citation: Vermont University Center for X-Ray Crystallography Core Facility (RRID:SCR_017688) Copy
http://biophysics.fsu.edu/facilities/protein-expression-facility/
Core to facilitate the large scale expression of recombinant proteins in bacterial, insects, and mammalian cells. Serves primarily faculty and students from the laboratories in the Kasha Laboratory Building and laboratories in Biology, Biochemistry, Chemistry and Nutrition at Florida State University, Tallahassee, FL.
Proper citation: Florida State University Protein Expression Core Facility (RRID:SCR_016757) Copy
https://www.rockefeller.edu/sbrc/
Core for protein expression and purification as well as all equipment needed for determination of three dimensional structures of biological macromolecules via X-ray crystallography. Houses Rigaku/MSC microMax 007HF generator for X-ray diffraction data collection, equipped with Varimax optics, X-stream 2000 cryosystems and two RaxisIV++ detectors.Also available is stereomicroscope, Nikon SMZ18, for crystal tray observations and crystal mounting., THIS RESOURCE IS NO LONGER IN SERVICE. Documented on September 16,2025.
Proper citation: Rockefeller University Structural Biology Resource Center Core Facility (RRID:SCR_017732) Copy
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