Anne Skaja Robinson

Anne Skaja Robinson joined Tulane University in January 2012 as the Chair of Chemical and Biomolecular Engineering. Prior to Tulane, Dr. Robinson was a Full Professor and Associate Chair at the University of Delaware, where she started her academic career. She earned her Bachelor’s and Master’s degrees in Chemical Engineering from the Johns Hopkins University. She earned her PhD in Chemical Engineering from the University of Illinois at Urbana-Champaign, and was an NIH postdoctoral fellow in the Department of Biology at MIT before joining the faculty at UD. Her honors include a DuPont Young Professor Award, and a National Science Foundation Presidential Early Career Award for Science and Engineering (PECASE) Award, and she is a fellow of the American Institute for Medical and Biological Engineering. She has several patents and over 70 publications in the field of biochemical engineering.

Research Interests

The Robinson laboratory is interested in understanding the fundamental interactions between molecules, both in isolation and in the complex environment of the cell. We use our growing understanding to design proteins with more robust or novel properties and to engineer cellular systems for improved production or drug screening applications. To this end, we are investigating the determinants of protein folding and misfolding, on both atomic and molecular levels. We have developed several novel approaches to inhibit protein misfolding and aggregation. Additionally, we are designing cellular systems for optimal expression of membrane proteins and antibodies.

A major goal of this research is to establish a set of cellular systems that could express any protein of interest. Recently, we have begun studies to understand the cellular interactions that lead to hyperphosphorylation and aggregation of tau protein, which is relevant to Alzheimer’s disease, and several other neurodegenerative diseases including corticobasal degeneration.

Our approach uses techniques in molecular biology, genetic engineering, and biophysical chemistry to identify and study macromolecules at both an atomic and cellular level. Mechanistic modeling guides us in experimental design and analysis. We use both prokaryotic (bacterial) systems as well as eukaryotic systems, such as yeast or mammalian cells. The research in the laboratory has focus areas in protein stability, expression, and aggregation for biotechnology and biomedical applications.

Publications Grouped (Most Recent 5 Years) – of Over 75 Total

Mass and Heat Transfer Textbook

Russell, T.W.F., Robinson, A.S., and Wagner, N.J., (2008) Mass and Heat Transfer: Analysis of Mass Contactors and Heat Exchangers, Cambridge University Press, Cambridge, UK (www.cambridge.org/9780521886703).

G-protein Coupled Receptors (7-Helix Transmembrane Proteins)

Naranjo, AN, A Chevalier, GD Cousins, E Ayettey, EC McCusker, C Wenk, AS Robinson (2015) Conserved disulfide bond is not essential for the adenosine A2A receptor: extracellular cysteines influence receptor distribution within the cell and ligand-binding recognition, BBA Biomembranes, 1848: 603-614 Available on-line Dec 5 2014 DOI: 10.1016/j.bbamem.2014.11.010.

Blocker, KM, ZT Britton, AN Naranjo, PM McNeely, CL Young, AS Robinson (2015) Recombinant G protein-coupled receptor expression in Saccharomyces cerevisiae for protein characterization, in "Membrane Proteins – Production and Function Characterization", Methods Enzymol., 556:165-83. doi: 10.1016/bs.mie.2014.12.025.

McNeely, P.M., Naranjo, A.N., and A.S. Robinson* (2012) Structure-function studies with G-protein coupled receptors as a paradigm for improving drug discovery and therapeutic development, Biotechnology Journal, 7(12): 1451-1461. DOI: 0.1002/biot.201200076.

Britton, Zachary T, Elizabeth I Hanle, and AS Robinson (2012) An Expression and Purification System for the Biosynthesis of Adenosine Receptor Peptides for Biophysical and Structural Characterization, Protein Exp. Purif., 84:224-235. PMID: 22722102.

O'Malley, Michelle A., Matthew E. Helgeson, Norman J. Wagner, Anne S. Robinson* (2011) “Toward Rational Design of Protein Detergent Complexes: Determinants of Mixed Micelles that are Critical for the in vitro Stabilization of a G-protein Coupled Receptor”, Biophysical Journal, 101 (8): 1938-1948. DOI: 10.1016/j.bpj.2011.09.018 PMID: 22004748.

Britton, Z., Young, C., Can, Ö., McNeely, P., Naranjo, A. and Robinson, A. S. (2012) Membrane Protein Expression in Saccharomyces cerevisiae, in Production of Membrane Proteins: Strategies for Expression and Isolation (ed A. S. Robinson), Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, Germany. doi: 10.1002/9783527634521.ch2.

Robinson, A.* (2011) “New Tools for Breaking Barriers to GPCR Expression in E. coli” Journal of Molecular Biology. 408 (4): 597-598.

O'Malley, MA, Helgeson, ME, Wagner, NJ and AS Robinson* (2011) Morphology and Composition of Cholesterol-rich Micellar Nanostructures Determine Transmembrane Protein (GPCR) Activity, Biophysical Journal, 100(2): L11-13.

O’Malley, MA, AN Naranjo, T Lazarova, AS Robinson* (2010) “Analysis of Adenosine A2a Receptor Stability: Effects of Ligands and Disulfide Bonds,” Biochemistry, Nov 2;49(43):9181-9.

Stress Response And Chaperone Interactions

Young, CL and AS Robinson* (2014) Protein Folding and Secretion: Mechanistic Insights Advancing Recombinant Protein Production in S. cerevisiae, Current Opinion in Biotechnology 30: 168-177. DOI: 10.1016/j.copbio.2014.06.018.

Griesemer, M., Young, C., Robinson, A.S., Petzold, L.* (2014) BiP Clustering Facilitates Protein Folding in the Endoplasmic Reticulum, PLOS Computational Biology, 10(7):1-16, 10.1371/journal.pcbi.1003675

Young, Carissa L., David L. Raden, Anne S. Robinson (2013) Analysis of ER Resident Proteins in S. cerevisiae: Implementation of H/KDEL Retrieval Sequences, Traffic, 14(4):365-81. DOI: 10.1111/tra.12041.

Young, Carissa L., David L. Raden, Jeffrey Caplan, Kirk Czymmek, Anne S. Robinson (2012) “Cassette Series Designed for Live-Cell Imaging of Proteins and High Resolution Techniques in Yeast”, Yeast, Mar;29(3-4):119-36. doi: 10.1002/yea.2895. Epub 2012 Apr 4. PMID: 22473760

Young, Carissa L., Zachary T. Britton, Anne S. Robinson (2012) “Recombinant Protein Expression and Purification: A Comprehensive Review of Affinity Tags and Microbial Applications” Biotechnology Journal, May;7(5):620-34. doi: 10.1002/biot.201100155. Epub 2012 Jan 10. PMID: 22442034

Griesemer, M, Young, CL, Doyle III, FJ, Robinson, AS and L Petzold (2011) Spatial Localization of Chaperone Distribution in the Endoplasmic Reticulum of Yeast, IET Systems Biology, 6(2):54-63. http://dx.doi.org/10.1049/iet-syb.2011.0006

Young C.L., Yuraszeck T., Robinson A.S.* (2011) “Decreased secretion and unfolded protein response upregulation,” Methods Enzymol. 491:235-60.

Spatara, ML and Robinson, A.S.* (2010) “Transgenic mouse and cell culture models demonstrate a lack of mechanistic connection between endoplasmic reticulum stress and tau dysfunction” Journal of Neuroscience Research, 88(9):1951-61. PMID: 20143409

Yuraszeck, T.M., Neveu, P., Rodriguez-Fernandez, M., Robinson, A.S., Kosik, K.S., Doyle III, F.J.* (2010) "Vulnerabilities in the Tau Network and The Role of Ultrasensitive Points in Tau Pathophysiology", PLoS Computational Biology, 6(11): e1000997. doi:10.1371/journal.pcbi.1000997 (with cover art).

Protein Aggregation and Refolding Studies

Wu, H, K Truncali, J Ritchie, R Kroe-Barrett, S Singh, AS. Robinson, and CJ Roberts* (2015) Weak protein interactions and pH- and temperature-dependent aggregation of human Fc1, mAbs, in press.

Wu, H., Rachel Kroe-Barrett, Sanjaya Singh, Anne S. Robinson, Christopher J. Roberts* (2014) Competing aggregation pathways for monoclonal antibodies, FEBS Letters 588(6): 936-941 http://dx.doi.org/10.1016/j.febslet.2014.01.051

Maurer, Ronald W., Alan K Hunter, Anne S. Robinson*, and Christopher J. Roberts* (2014) Aggregates of alpha-chymotrypsinogen anneal to access more stable states, Biotechnology & Bioengineering, 111 (4): 782-791. doi: 10.1002/bit.25129 PMID: 24122552

Maurer, Ronald W., Alan K Hunter, Xiangyang Wang, William K Wang, Anne S. Robinson, and Christopher J. Roberts* (2013) Folding and aggregation of a multi-domain engineered immunotoxin, Biochemical Engineering Journal, 81: 8-14. http://dx.doi.org/10.1016/j.bej.2013.09.015 .

Blanco, Marco, Sahin, Erinc, Robinson, Anne, Roberts, Christopher* (2013) Coarse-Grained Model for Colloidal Protein Interactions, B22, and Protein Cluster Formation, The Journal of Physical Chemistry, Part B, Dec 19;117(50):16013-28. doi: 10.1021/jp409300j PMID: 24289039

JA Costanzo, CJ O’Brien, K Tiller, E Tamargo, AS Robinson, CJ Roberts, and EJ Fernandez,* (2013) Computational Design to Control Protein Aggregation Rates Through Conformational Stability, Protein Eng, Des, & Sel, 27 (5): 157-167 10.1093/protein/gzu008

Morozova, Olga A, Zachary M March, Anne Skaja Robinson, and David W. Colby* (2013) Conformational features of tau fibrils from Alzheimer's disease brain are faithfully propagated by unmodified recombinant protein, Biochemistry, 52(40):6960-7. http://dx.doi.org/10.1021/bi400866w PMID: 24033133

Sahin, E., Jordan, J.L., Spatara, M.L., Naranjo, A.N., Weiss IV, W.F., Robinson, A.S, Fernandez, E.J.*, Roberts, C.J.* (2011) “Computational Design and Biophysical Characterization of Aggregation-Resistant Point Mutations for γD Crystallin Illustrate a Balance of Conformational Stability and Intrinsic Aggregation Propensity”, Biochemistry, Feb 8;50(5):628-39.

Other Publications

St. Amand, Melissa M., Devesh Radhakrishnan, Anne S. Robinson, Babatunde. A. Ogunnaike* (2014) Identification of Manipulated Variables for a Glycosulation Control Strategy, Biotech Bioeng, Oct;111(10):1957-70. doi: 10.1002/bit.25251.

St. Amand, Melissa M., Kevin Tran, Devesh Radhakrishnan, Anne S. Robinson, Babatunde. A. Ogunnaike* (2014) Controllability Analysis of Protein Glycosylation in CHO cells, PLoS One, 9(2): e87973. DOI: 10.1371/journal.pone.0087973

St. Amand, Melissa, Ogunnaike, Babatunde A., and Robinson, Anne S.* (2014) Development of At-Line Assay to Monitor Charge Variants of mAbs During Production, Biotechnology Progress, 30: 249–255. DOI: 10.1002/btpr.1848 PMID: 24382831