Welcome to the R. L. Juliano Structural Bioinformatics Core facility at the University of North Carolina at Chapel Hill. The Director of this Core, Dr. Brenda Temple, is available for consultations and collaborations on research studies requiring computational structural biology methods.
One type of study includes combining 3D structure analysis and sequence analysis with phylogenetic or molecular evolution methods for the identification of functionally and structurally important residues. Molecular modeling studies, whereby the structure of the protein of interest is predicted using known experimental structures, provide 3D atomic data when no experimental structure is available. Molecular dynamics studies are tools for analyzing the role of dynamic motion as well as structure in protein function. Output from these studies include but are not limited to analyses of collective motions within macromolecules. These types of analyses allow the researcher to identify critical residues relating structure to function. These structure/function studies further lead to development of hypotheses testable in the laboratory.
For more information on what services are available go to General Information.
To learn about available software packages go to Computational Tools.
For examples of current research using our tools, please visit Research Applications.
1. McClain B, Settembre E, Temple BR, Bellamy AR, Harrison SC (2010). X-ray crystal structure of the rotavirus inner capsid particle at 3.8 Å resolution. J Mol Biol, 397(2):587-99. PMCID: PMC2860780
2. Kwak YT, Raney A, Kuo LS, Denial SJ, Temple BR, Garcia JV, Foster JL (2010). Self-association of the Lentivirus protein, Nef. Retrovirology, 7(1):77 PMCID: PMC2955668
3. Dibble CF, Horst JA, Malone MH, Park K, Temple B, et al. (2010). Defining the Functional Domain of Programmed Cell Death 10 through Its Interactions with Phosphatidylinositol-3,4,5-Trisphosphate. PLoS ONE 5(7): e11740. doi:10.1371/journal.pone.0011740. PMCID: PMC2909203
4. Temple BR, Jones CD, Jones AM (2010). Evolution of a signaling nexus constrained by protein interfaces and conformational states. PLoS Comput Biol 6(10):e1000962. PMCID: PMC2954821
5. Hamel B, Monaghan-Benson E, Rojas RJ, Temple BRS, Marston DJ, Burridge K, Sondek J (2011). SmgGDS is a guanine nucleotide exchange factor that specifically activates RhoA and RhoC. J Biol Chem. Apr 8;286(14):12141-8. PMCID: PMC3069418
6. Jones JC, Duffy JW, Machius M, Temple BRS, Dohlman HG, Jones AM (2011). The crystal structure of a self-activating G Protein a subunit reveals its distinct mechanism of signal initiation. Sci. Signal. 4, ra8.
7. Jones JC, Temple BR, Jones AM, Dohlman HG (2011). Functional reconstitution of an atypical G protein heterotrimer and regulator of G protein signaling protein (RGS1) from Arabidopsis thaliana. J Biol Chem. Apr 15;286(15):13143-50. PMCID: PMC3075661
8. Foster JL, Denial SJ, Temple BR, Garcia JV (2011). Mechanisms of HIV-1 Nef Function and Intracellular Signaling. J Neuroimmune Pharmacol. 2011 Jun;6(2):230-46.
9. Friedman EJ, Wang HX, Jiang K, Perovic I, Deshpande A, Pochapsky TC, Temple BRS, Hicks SN, Harden TK, Jones AM (2011). Acidreductone dioxygenase 1 (ARD1) is an effector of the heterotrimer G protein beta subunit in Arabidopsis. J Biol Chem. Aug 26;286(34):30107-18.