Â鶹¹ú²úAV

Ph.D. in Biochemistry, University of Miami, (1998)

B.S. in Microbiology, University of Miami, (1991)

Expertise

Research Interests

1. Protein Chemistry2. Molecular Biology and Genetic Engineering3. Bioinformatics and Genomics4. Protein Evolution5. Biophysics: Multidimensional heteronuclear NMR, Real-time 1D NMR & Photo-CIDNP, Circular dichroism & Fluorescence spectroscopy (equilibrium & stopped flow); Quenched flow HX.

Articles

Collins, J. C., Bedford, J. T. and Greene, L. Hope. (2016). Elucidating the Key Determinants of Structure, Folding, and Stability for the (4 beta-alpha) Conformation of the B1 Domain of Protein G Using Bioinformatics Approaches. IEEE transactions on nanobioscience.

Greene, L. Hope., Li , H., Zhong, J., Zhao, G. and Wilson, K. (2012). Folding of an all-helical Greek-key protein monitored by quenched-flow hydrogen-deuterium exchange and NMR spectroscopy. European biophysics journal (EBJ) 41 (1) , pp. 41-51.

Greene, L. Hope. and Grant, T. (2012). Protein folding by 'levels of separation': a hypothesis. FEBS letters 586 (7) , pp. 962-6.

Collins, J. C. and Greene, L. Hope. (2012). Biophysical analysis of the transition of an all α-helical Greek-key protein into amyloid fibrils composed of β-sheet structure. Protein and peptide letters 19 (9) , pp. 982-90.

Greene, L. Hope. (2012). Protein structure networks. Briefings in functional genomics 11 (6) , pp. 469-78.

Li, H. and Greene, L. Hope. (2010). Sequence and structural analysis of the chitinase insertion domain reveals two conserved motifs involved in chitin-binding. PLoS One 13 , pp. e8654.

Li, H., Wojtaszek, J. and Greene, L. Hope. (2009). Analysis of conservation in the Fas-associated death domain protein and the importance of conserved tryptophans in structure, stability, and folding. Biochmica et Biophysica Acta - Proteins & Proteomics 1794 , pp. 583-593.

Higman, V. A., Rosner, H. I., Ugolini, R., Greene, L. Hope., Redfield, C. and Smith, L. J. (2009). Probing the urea dependence of nonrandom interactions in denatured human α-lactalbumin. J. Biomolecular NMR 45 , pp. 121-131.

Cuff, A., Redfern, O. C., Greene, L. Hope., Sillitoe, I., Lewis, T., Dibley, M., Reid, A., Pearl, F., Dallman, T., Todd, A., Garratt, R., Thornton, J. and Orengo, C. (2009). The CATH hierarchy revisited - structural divergence in domain superfamilies and the continuity of fold space. Structure 17 , pp. 1051-1062.

Greene, L. Hope., Lewis, T. E., Addou, S., Cuff, A., Dallman, T., Dibley, M., Redfern, O., Pearl, F., Nambudiry, R., Reid, A., Sillitoe, L., Yeats, C., Thornton, J. M. and Orengo, C. A. (2007). The CATh domain structure database: new protocols and classification levels give a more comprehensive resource for exploring evolution. Nucleic Acids Research 35 , pp. D291-D297.

Greene, L. Hope., Wijesinha-Bettoni, R. and Redfield, C. (2006). Characterization of the molten globule of human-serum retinol-binding protein by NMR spectroscopy. Biochemistry 45 , pp. 9475-9484.

Higman, V. A. and Greene, L. Hope. (2006). Elucidation of conserved long-range interaction networks in proteins and their significance in determining protein topology. Physica A , pp. 595-606.

Paci, E., Greene, L. Hope., Jones, R. M. and Smith, L. J. (2005). Characterization of the molten globule state of retinol-binding protein using a molecular dynamics simulation approach. FEBS J 272 , pp. 4826-4838.

Greene, L. Hope. and Higman, V. A. (2005). Conserved networks and the determinants of protein topology. FEBS J 272 , pp. Suppl. 1.

Neerathilingam, M., Greene, L. Hope., Colebrooke, S. A., Campbell, I. D. and Staunton, D. (2005). Quantitation of protein expression in a cell-free system: Efficient detection of yields and 19F NMR to identify folded protein. J Biomolecular NMR 31 , pp. 11-19.

Greene, L. Hope., Hamada, D., Eyles, S. J. and Brew, K. (2003). Conserved signature proposed for folding in the lipocalin superfamily. FEBS letters 553 (1-2) , pp. 39-44.

Greene, L. Hope. and Higman, V. A. (2003). Uncovering network systems within protein structures. Journal of molecular biology 334 (4) , pp. 781-91.

McCammon, M. G., Scott, D. J., Keetch, C. A., Greene, L. Hope., Purkey, H. E., Petrassi, H. M., Kelly, J. and Robinson, C. V. (2002). Screening transthyretin amyloid fibril inhibitors: characterization of novel multiprotein, multiligand complexes by mass spectrometry. Structure (London, England : 1993) 10 (6) , pp. 851-63.

Greene, L. Hope., Chrysina, E. D., Irons, L. I., Papageorgiou, A. C., Acharya, K. R. and Brew, K. (2001). Role of conserved residues in structure and stability: tryptophans of human serum retinol-binding protein, a model for the lipocalin superfamily. Protein science : a publication of the Protein Society 10 (11) , pp. 2301-16.

Greene, L. Hope., Grobler, J. A., Malinovskii, V. A., Tian, J., Acharya, K. R. and Brew, K. (1999). Stability, activity and flexibility in alpha-lactalbumin. Protein engineering 12 (7) , pp. 581-7.

Book Chapters

Collins, J. and Greene, L. Hope. (2013). Conversion of all α-helical proteins into an alternative β-amyloid conformation Bio-nanoimaging – Protein Misfolding and Aggregation. (pp. 485-501) Academic Press.

Gaforina, L., Sanchez, D., Greene, L. Hope. and Flower, D. R. (2006). The lipocalin protein family: Protein sequence and structure Lipocalins Georgetown, TX: Landes Biosciences and Eurekha.com.

Presentations

Barnes, C., Greene, L. Hope. and Lee, J. (March , 2019). Assessing the stability and expression of transgenes in genetically engineered cyanobacteria for biofuel production Poster 257th American Chemical Society Orlando, FL.

Sacko, O., Barnes, C., Greene, L. Hope. and Lee, J. (March , 2019). Survivability of genetically engineered Thermosynechococcus elongatus BP1 in different temperature conditions Poster 257th American Chemical Society Orlando, FL.

Haratipour, Z., Poutsma, J. and Greene, L. (March , 2019). Conserved long-range interaction networks, energetics and the determinants of protein topology Oral Presentation 257th American Chemical Society National Meeting Orlando, FL.

Bedford, J., Poutsma, J. and Greene, L. (May , 2018). Persistence of key long-range interactions during GB1 unfolding simulations Oral Presentation 96th Annual Meeting of the Virginia Academy of Science .

Haratipour, Z. (March , 2018). Characterization of long-range interaction networks in proteins using key network principles Oral Presentation 255th American Chemical Society National Meeting .

Beford, J., Greene, L. and Poutsma, J. (March , 2018). Computational exploration of the β-grasp fold for structure, function, and stability Oral Presentation 255th American Chemical Society National Meeting .

Haratipour, Z. and Greene, L. (May , 2017). The significance of the conserved long-ranged interaction networks in determining protein topology Oral Presentation The 95th Virginia Academy of Sciences Annual Meeting .

Greene, L. Hope. (November , 2010). Greensboro, NC.

Greene, L. Hope. (June , 2010). International Conference on Cold Plasma in Medicine Norfolk, VA.

Greene, L. Hope. (August , 2009). 238th American Chemical Society National Conference Washington, DC.

Greene, L. Hope. (April , 2009). Conserved Protein Structure Networks Rock Hill, SC.

Greene, L. Hope. (October , 2008). Computational approaches to study protein structure and folding Hampton, VA.

Greene, L. Hope. (October , 2008). Conserved Protein Structure Networks Shippensburg, PA.

Greene, L. Hope. (October , 2008). Protein structure networks and the fold continuum Ashland, VA.

Greene, L. Hope. (April , 2008). Computational approaches to study protein structure and folding Norfolk, VA.

Greene, L. Hope. (March , 2008). Computational approaches to study protein structure and folding Lexington, VA.

Greene, L. Hope. (April , 2007). Computational approaches to study protein structure and folding Fairfax, VA.

Greene, L. Hope. (April , 2007). Computational approaches to study protein structure and folding Norfolk, VA.

Greene, L. Hope. (September , 2006). 'Bioinformatics to Proteomics' Course London, UK.

Greene, L. Hope. (July , 2005). 30th FEBS Congress and 9th IUBMB Conference on Proteins Budapest, Hungary.

• 2017: John R. Broderick Diversity Champion Award, Â鶹¹ú²úAV President
• 2010: Most Inspiring Faculty Mentor, Department of Chemistry and Biochemistry (Top Graduating Biochemistry Senior)
• 2009: Most Inspiring Faculty Mentor, Department of Chemistry and Biochemistry (Top Graduating Biochemistry Senior)