Natural Science Faculty

Apply Now

Learn More

Visit Us


Dr. Linda Luck

Professor of Biochemistry

My research laboratory is located in Hudson Annex at SUNY Plattsburgh and my goals are to understand how structure relates to function in biological molecules. In particular we are interested in studying how conformational changes that take place in proteins affect biological events such as the onset of breast cancer. In my laboratory we use proteins ranging from bacteria and human proteins including the estrogen receptor and androgen receptor. Recently we have developed biosensors from these proteins. My laboratory students use an array of methods spanning biophysics, biochemistry, protein engineering, and molecular biology. My students have access to modern tools of chemistry and biology including fluorescence, NMR, mass spectrometry, X-ray crystallography, electrochemistry, and molecular graphics.



The Human Estrogen Receptor and Cancer

A present focus of my research is to explain the molecular basis for reproductive cancers especially breast cancer. Activation and control of the estrogen receptor play a critical role in both the development and progression of breast cancer. Transcriptional activation is thought to be stimulated via a ligand-dependent conformational change when ligands bind to the estrogen receptor. It is critical that we understand the molecular details of the interactions between the estrogen receptor and estradiol, antiestrogens and environmental estrogens. Although a crystal structure has provided us with a static picture of the hormone-binding domain of the estrogen receptor these data have not addressed the conformational changes that mediate the transcriptional events within the nucleus. We are investigating the use of NMR experiments to provide a greater understanding of how structurally diverse estrogens and antiestrogens interact with the estrogen receptor.

Biosensors for Endocrine Disruptors

Our laboratory is exploring the use of a Quartz Crystal Microbalance as a biosensor for the xenobiotic compounds that bind to the Estrogen and Androgen hormone receptors. One of the interesting and impending characteristics of the steroid receptors is their ability to tolerate large changes in ligand structure. A wide variety of diverse nonsteriodal compounds exhibit high affinity binding towards the steroid receptors, from such structural classes as pyrazole, stilbestrol, coumarin, isoflavones, and benzofurans. The behavior of compounds with respect to their steroid binding properties has proven difficult to predict because surprisingly, many bear no resemblance to endogenous steroids. Because such a diversity of compounds exhibit steroid behavior, and these compounds produce such dramatic and systemic effects, it is essential that we test new compounds before they are released into the environment where their effects on human and wildlife health could be enormous.

Got a question for Linda?

Contact her at


  • Ph.D. in Chemistry, University of Vermont, Burlington, 1989
    Thesis title: Stereodynamics of Platinum Phosphine Complexes
  • M.A. in Chemistry, State University of New York, Plattsburgh, 1980
    Thesis title: The Purification of Elongation Factor II in Protein Biosynthesis
  • B.A. in Chemistry, State University of New York, Potsdam, 1974
  • Medical Technology Internship 1973–1974, Medical Center at Princeton, Princeton, NJ
    American Society of Clinical Pathologists Registered Medical Technologist
  • Postdoctoral Training:
    • Department of Chemistry/Biochemistry, University of Colorado, Boulder
    • Department of Chemistry, University of Wisconsin, Madison
    • Department of Biochemistry, Medical School, University of Vermont

Teaching Areas

  • Biochemistry
  • Physical Biochemistry
  • Kitchen Chemistry: Molecular Gastronomy


  • SUNY Chancellor's Award for Excellence in Scholarship and Creative Activities, 2012
  • Featured Scholar, Celebration of Scholarship, SUNY Plattsburgh, 2010
  • Participant in COACh Professional Skills Development for Women Faculty, 2002 and 2003
  • Graham Research Faculty Award, 2000
  • Finn Wold Travel Award-Protein Society, 1996
  • Participant in AAMC Professional Development Seminar for Junior Women Faculty, 1992


  • DURIP DOD /ARO “Purchase of a NanoHPLC (UPLC) for the Advancement of Proteomics Research at Clarkson University and SUNY Plattsburgh” 2011–2014 $107,435
  • President’s Award “19F NMR Studies of the Estrogen Receptor” 2011–2012 $5,000
  • SUNY Mini Grant “Mass Spectrometry of Proteins” 2011 $1200
  • UUP Professional Development Individual Awards Program 2008–09
  • Educational Technology Grant SUNY “Using the Personal Computer and Internet for Biochemistry Education in the Laboratory” 2009–2010 $23,000
  • SUNY Curriculum Development Proposal for the Professional Science Master’s Program $10,000 Project Team Leader for the Allied Health Initiative
  • NSF MRI “Acquisition of an LCMS for the Chemistry Department at the University of Vermont” $430,000 2008–2011 Co PI
  • Educational Technology Grant SUNY “Green Chemistry: Effective Education using Computer Simulations and Calculations” 2007 Co-PI with Dr. Ed Miller $50,000
  • UUP Professional Development Individual Awards Program 2006–07
  • DOD BRCP“Development of a Biosensor for Identifying Novel Endocrine Disrupting Chemicals” 2007–2009 $93,000 CO-PI with Silent Spring Institute, Newton, MA
  • NSF “Summer supplement for High School Teacher for Electrochemical Impedence Architecture for Biosensors” Co-PI with Ian Suni 2006–2007 $10,000
  • NSF “Electrochemical Impedance Architecture for Biosensors” Co-PI with Ian Suni 2003–2007 $300,000
  • NSF Funded Faculty Associate-K-12 Project Based Learning Partnership Program 2000–2002 $48,688
  • NIH RO3 “Estrogenic Substance Detection by a Modified Nanobalance” PI 2001–2004 $146,308
  • PRF ACS-AC “Probing the Dynamic Behavior of the Human Estrogen Receptor by 19F NMR” PI 2001–2004 $60,000
  • Heart and Stroke Canada Research Grant OAI-1 “Structure Function and Interaction Studies” Co-PI with Art Szabo University of Waterloo, Toronto CA 2001–2002 $25,000

Selected Recent Publications

  • Luck, L. A., & Blondo, R. M. (2012). The grapes of class: Teaching chemistry concepts at a winery. Journal of Chemical Education, 89(10), 1264–1266.
  • Roy, U & Luck, L.A. (2011) Cysteine residues in receptor proteins: Structural insights from two E. coli periplasmic receptors. Journal of Chemistry and Chemical Engineering, 5, 771–777.
  • Andreescu, S. & Luck, L. A. (2008). Genetically engineered protein films on gold nanoparticles: A novel electrochemical glucose biosensor. Analytical Biochemistry, 375, 282–290.
  • Roy, U., & Luck, L. A. (2007). Molecular modeling of estrogen receptor using molecular operating environment. Biochemistry and Molecular Biology Education, 35(4), 238–243.
  • Wang, J., Luck, L. A., & Suni, I. I. (2007). Immobilization of the glucose-galactose receptor protein onto a au electrode through a genetically engineered Cysteine residue. Electrochemical and Solid-State Letters, 10(2), 133–136.
  • Tripathi, A., Wang, J., Luck, L. A., & Suni, I. I. (2007). Nanobiosensor design utilizing a periplasmic E. coli receptor protein immobilized within au/polycarbonate nanopores. Analytical Chemistry, 79(3), 1266–1270.
  • Baltus, R. E., Carmon, K. S., & Luck, L. A. (2007). Quartz crystal microbalance with immobilized protein receptors: Comparison of response to ligand binding for direct protein immobilization and protein attachment via disulfide linker. Langmuir, 23, 3990–3995.
  • Sokolov, I., Subba-Rao, V., & Luck, L. A. (2006). Change in rigidity in the activated form of the glucose/galactose receptor from E. coli: A phenomenon that will be key to the development of piezoelectric biosensors. Biophysical Journal, 90(3), 1055–1063.
  • Carmon, K. S., Baltus, R. E., & Luck, L. A. (2005). A biosensor for estrogenic substances using the quartz crystal microbalance. Analytical Biochemistry, 345(2), 277–283.
  • Wang, J., Carmon, K. S., Luck, L. A., & Suni, I. I. (2005). Electrochemical impedance biosensor for glucose detection utilizing a periplasmic E. coli receptor protein. Electrochemical and Solid-State Letters, 8(8), 61–64.
  • Carmon, K. S., Baltus, R. E., & Luck, L. A. (2004). A piezoelectric quartz crystal biosensor: The use of two single cysteine mutants of the periplasmic E. coli glucose/galactose receptor as target proteins for the detection of glucose. Biochemistry, 43(44), 14249–14256.
  • Abbott, G. L., Blouse, G. E., Perron, M. J., Shore, J. D., Luck, L. A., & Szabo, A. G. (2004). 19 F NMR studies of plasminogen sctivator inhibitor-1. Biochemistry, 43(6), 1507–1519.
  • Magnusson, U., Salopek-Sondi, B., Luck, L. A., & Mowbray, S. L. (2004). X-ray structures of the leucine-binding protein illustrate conformational changes and the basis of ligand specificity. Journal of Biological Chemistry, 279, 8747–8752.
  • Luck, L. A., Moravan, M. J., Garland, J. E., Salopek-Sondi, B., & Roy, D. (2003). Chemisorptions of bacterial receptors for hydrophobic amino acids and sugars on gold for biosensor applications: A surface plasmon resonance study of genetically engineered proteins. Biosensors and Bioelectronics, 19(3), 249–259.
  • Salopek-Sondi, B., Skeels, M. C., Swartz, D., & Luck, L. A. (2003). Insight into the stability of the hydrophobic binding proteins of E. coli: Assessing the proteins for use as biosensors. Proteins: Structure, Function, and Genetics, 53(2), 273–281. doi:10.1002/prot.10485
  • Salopek-Sondi, B., Vaughan, M. D., Skeels, M. C., Honek, J. F., & Luck, L. A. (2003). 19 F NMR studies of the leucine-isoleucine-valine binding protein: Evidence that a closed conformation exists in solution. Journal of Biomolecular Structure and Dynamics, 21(2), 235–246.
  • Salopek-Sondi, B., Swartz, D., Adams, P. S., & Luck, L. A. (2002). Exploring the role of amino acid-18 of the leucine binding proteins of E. coli. Journal of Biomolecular Structure and Dynamics, 20(3), 381–387.
  • Salopek-Sondi, B., & Luck, L. A. (2002). 19F NMR study of the L-leucine-specific binding protein of Escherichia coli: Mutagenesis and assignment of the 5-fluorotryptophan-labeled residues. Protein Engineering Design and Selection, 15, 857-861.
  • Senear, D. F., Mendelson, R. A., Stone, D. B., Luck, L. A., Rusinova, E., & Ross, J. B. A. (2002). Quantitative analysis of Tryptophan analogue incorporation in recombinant proteins. Analytical Biochemistry, 300(1), 77–86.
  • Luck, L. A., Barse, J. L., Luck, A. M. & Peck, C. (2000). Conformational changes in the human estrogen receptor observed by fluorine NMR.  Biochemical Biophysical Research Communications, 270, 988–991.
  • Luck, L. A. & Johnson, C. (2000). Fluorescence and 19F NMR evidence that phenylalanine and 4-L-fluorophenylalanine bind to the L-leucine specific receptor of E. coli. Protein Science, 9, 2573–2576.

Contact Linda Luck

Office: Hudson Hall 233
Phone: (518) 564-4119