10) Protein Interactions Core (Mvszka. Director)OverviewOur Protein Interaction Core will tap into an existing Core facility that is part of the University of Utah'sHealth Sciences Core facilities. The Protein Interaction Core facility was established in 1996 to provideinternal and external academic users access to state-of-the-art, label-free, real-time interactiontechnologies. Over the past 10 years, this facility has contributed to more than 100 research projectsthat encompass a wide array of biological areas.The Protein Interaction Core is centrally located within the School of Medicine (Rm 4A416) on theHealth Sciences campus. The laboratory's 1600 square feet of space was entirely renovated in 1997and was specifically designed to accommodate the Core facility's equipment and personnel. Currently,the facility maintains 7 surface plasmon resonance-based optical biosensors: 3 Biacore 2000s, 1 Biacore3000, 1 Biacore S51, 1 Biacore Flexchip, and 1 Lumera Proteome Processor. The Biacore 2000/3000platforms are ideal for measuring protein-protein interactions, while the Biacore S51 is designed forsmall-molecule interaction analysis. The Flexchip and Proteome Processor instruments are array-basedimaging systems that allow one to study up to 1000 binding partners immobilized onto the sensorsurface at one time. The Core has worked closely with both Biacore and Lumera on the development ofthis new hardware, as well as data analysis software. In early 2007, we plan to add a new biosensor(the ProteOn XPR36 from BioRad Laboratories) to our Core, funded by ab NIH Shared InstrumentGrant. Together, these state-of-the-art instruments allow us to measure the interactions of biomoleculessuch as proteins, oligonucleotides, and lipids in high-resolution, as well as high-throughput, formats.Experiments are scheduled through email contacts with the Core's manager. Typically, the investigatorand their staff then meet with the manager to plan the best course of action for the proposed study.Samples are then dropped off at the Core and experiments are initiated the same day. This ensures thatlabile samples are able to be processed in a timely manner.

National Institute of Health (NIH)
National Institute of General Medical Sciences (NIGMS)
Specialized Center (P50)
Project #
Application #
Study Section
Special Emphasis Panel (ZRG1-AARR-A (40))
Project Start
Project End
Budget Start
Budget End
Support Year
Fiscal Year
Total Cost
Indirect Cost
University of Utah
Salt Lake City
United States
Zip Code
Coey, Aaron T; Larsen, Kevin P; Choi, Junhong et al. (2018) Dynamic Interplay of RNA and Protein in the Human Immunodeficiency Virus-1 Reverse Transcription Initiation Complex. J Mol Biol 430:5137-5150
Swulius, Matthew T; Nguyen, Lam T; Ladinsky, Mark S et al. (2018) Structure of the fission yeast actomyosin ring during constriction. Proc Natl Acad Sci U S A 115:E1455-E1464
Hammond, John A; Zhou, Li; Lamichhane, Rajan et al. (2018) A Survey of DDX21 Activity During Rev/RRE Complex Formation. J Mol Biol 430:537-553
Wang, Haoqing; Barnes, Christopher O; Yang, Zhi et al. (2018) Partially Open HIV-1 Envelope Structures Exhibit Conformational Changes Relevant for Coreceptor Binding and Fusion. Cell Host Microbe 24:579-592.e4
Pastuzyn, Elissa D; Day, Cameron E; Kearns, Rachel B et al. (2018) The Neuronal Gene Arc Encodes a Repurposed Retrotransposon Gag Protein that Mediates Intercellular RNA Transfer. Cell 172:275-288.e18
Wagner, Jonathan M; Christensen, Devin E; Bhattacharya, Akash et al. (2018) General Model for Retroviral Capsid Pattern Recognition by TRIM5 Proteins. J Virol 92:
Donaldson, G P; Ladinsky, M S; Yu, K B et al. (2018) Gut microbiota utilize immunoglobulin A for mucosal colonization. Science 360:795-800
Bailey, Lucas J; Sheehy, Kimberly M; Dominik, Pawel K et al. (2018) Locking the Elbow: Improved Antibody Fab Fragments as Chaperones for Structure Determination. J Mol Biol 430:337-347
Pak, Alexander J; Voth, Gregory A (2018) Advances in coarse-grained modeling of macromolecular complexes. Curr Opin Struct Biol 52:119-126
Redman, Joseph S; Francis, J Nicholas; Marquardt, Robert et al. (2018) Pharmacokinetic and Chemical Synthesis Optimization of a Potent d-Peptide HIV Entry Inhibitor Suitable for Extended-Release Delivery. Mol Pharm 15:1169-1179

Showing the most recent 10 out of 180 publications