N. Karl Maluf. PH.D

Senior Scientist 



Before joining APL in 2013 Karl was an Assistant Professor in the Department of Pharmaceutical Sciences at University of Colorado Denver for 6 years, where he studied virus assembly and DNA-protein interactions via AUC, fluorescence, stopped-flow kinetics, and other biophysical, biochemical, and thermodynamic approaches.

Prior to that Karl did postdoctoral work at U.C. Denver with Dr. Carlos Catalano and at the University of Iowa with Dr. Michael Feiss. Karl obtained his Ph.D. in Molecular Biophysics at Washington University School of Medicine under Dr. Timothy Lohman in 2003.

Karl has authored 28 scientific publications, listed here, including 13 involving AUC.


Yang, T. C., Catalano, C. E., and Maluf, N. K. (2015). Analytical Ultracentrifugation as a Tool to Study Nonspecific Protein-DNA Interactions. Methods Enzymol. 562, 305-330.


Tarasevich, B. J., Philo, J. S., Maluf, N. K., Krueger, S., Buchko, G. W., Lin, G., and Shaw, W. J. (2015). The leucine-rich amelogenin protein (LRAP) is primarily monomeric and unstructured in physiological solution. J. Struct. Biol. 190, 81-91.


Yang, T. C and Maluf, N. K. (2014). Characterization of the non-specific DNA binding properties of the Adenoviral IVa2 protein. Biophys. Chem. 194, 1-8.


Rudolph, M. C., Wellberg, E. A., Lewis, A. S., Terrell, K. L., Merz, A. L., Maluf, N. K., Serkova, N. J., and Anderson, S. M. (2014). Thyroid Hormone Responsive Protein Spot14 Enhances Catalysis of Fatty Acid Synthase in Lactating Mammary Epithelium. J. Lipid Res. 55, 1052-1065.


Bain, D. L., Connaghan, K. D., Maluf, N. K., Yang, Q., Miura, M. T., De Angelis, R. W., Degala, G. D., and Lambert, J. R. (2013). Steroid receptor-DNA interactions: toward a quantitative connection between energetics and transcriptional regulation. Nucleic Acids Res. (epub ahead of print)[free full text]


Connaghan, K. D., Miura, M. T., Maluf, N. K., Lambert, J. R., and Bain, D. L. (2013). Analysis of a glucocorticoid-estrogen receptor chimera reveals that dimerization energetics are under ionic control. Biophys. Chem. 172, 8-17.


Bain, D. L., Yang, Q., Connaghan, K. D., Robblee, J. P., Miura, M. T., Degala, G. D., Lambert, J. R., and Maluf, N. K. (2012). Glucocorticoid receptor-DNA interactions: binding energetics are the primary determinant of sequence-specific transcriptional activity. J. Mol. Biol. 422, 18-32.


Yang, T. C. and Maluf, N. K. (2012). Cooperative heteroassembly of the adenoviral L4-22K and IVa2 proteins onto the viral packaging sequence DNA. Biochemistry 51, 1357-1368.


Jia, H., Korolev, S., Niedziela-Majka, A., Maluf, N. K., Gauss, G. H., Myong, S., Ha, T., Waksman, G., and Lohman, T. M. (2011). Rotations of the 2B sub-domain of E. coli UvrD helicase/translocase coupled to nucleotide and DNA binding. J. Mol. Biol. 411, 633-648.


Maluf, N. K. and Yang, T. C. (2011). Thermodynamic linkage of large-scale ligand aggregation with receptor binding. Biophys. Chem. 154, 82-89.


Niedziela-Majka, A., Maluf, N. K., Antony, E., and Lohman, T. M. (2011). Self-assembly of Escherichia coli MutL and its complexes with DNA. Biochemistry 50, 7868-7880.


Tomko, E. J., Jia, H., Park, J., Maluf, N. K., Ha, T., and Lohman, T. M. (2010). 5'-Single-stranded/duplex DNA junctions are loading sites for E. coli UvrD translocase. EMBO J. 29, 3826-3839. [free full text]


Yang, T. C. and Maluf, N. K. (2010). Self-association of the adenoviral L4-22K protein. Biochemistry 49, 9830-9838.


Yang, Q., Catalano, C. E., and Maluf, N. K. (2009). Kinetic analysis of the genome packaging reaction in bacteriophage lambda. Biochemistry 48, 10705-10715.


Yang, T. C., Yang, Q., and Maluf, N. K. (2009). Interaction of the adenoviral IVa2 protein with a truncated viral DNA packaging sequence. Biophys. Chem. 140, 78-90.


Townsend, H. L., Jha, B. K., Han, J. Q., Maluf, N. K., Silverman, R. H., and Barton, D. J. (2008). A viral RNA competitively inhibits the antiviral endoribonuclease domain of RNase L. RNA 14, 1026-1036.


Yang, Q., Maluf, N. K., and Catalano, C. E. (2008). Packaging of a unit-length viral genome: the role of nucleotides and the gpD decoration protein in stable nucleocapsid assembly in bacteriophage lambda. J. Mol. Biol. 383, 1037-1048.


Maluf, N. K. and Feiss, M. (2006). Virus DNA translocation: progress towards a first ascent of mount pretty difficult. Mol. Microbiol. 61, 1-4. [free PDF]


Maluf, N. K., Gaussier, H., Bogner, E., Feiss, M., and Catalano, C. E. (2006). Assembly of bacteriophage lambda terminase into a viral DNA maturation and packaging machine. Biochemistry 45, 15259-15268.


English, C. M., Maluf, N. K., Tripet, B., Churchill, M. E., and Tyler, J. K. (2005). ASF1 binds to a heterodimer of histones H3 and H4: a two-step mechanism for the assembly of the H3-H4 heterotetramer on DNA. Biochemistry 44, 13673-13682.


Gaussier, H., Ortega, M. E., Maluf, N. K., and Catalano, C. E. (2005). Nucleotides regulate the conformational state of the small terminase subunit from bacteriophage lambda: implications for the assembly of a viral genome-packaging motor. Biochemistry 44, 9645-9656.


Maluf, N. K., Yang, Q., and Catalano, C. E. (2005). Self-association properties of the bacteriophage lambda terminase holoenzyme: implications for the DNA packaging motor. J. Mol. Biol. 347, 523-542.


Fischer, C. J., Maluf, N. K., and Lohman, T. M. (2004). Mechanism of ATP-dependent translocation of E.coli UvrD monomers along single-stranded DNA. J. Mol. Biol. 344, 1287-1309.


Lucius, A. L., Maluf, N. K., Fischer, C. J., and Lohman, T. M. (2003). General methods for analysis of sequential "n-step" kinetic mechanisms: application to single turnover kinetics of helicase-catalyzed DNA unwinding. Biophys. J. 85, 2224-2239. [free full text]


Maluf, N. K., Fischer, C. J., and Lohman, T. M. (2003). A Dimer of Escherichia coli UvrD is the active form of the helicase in vitro. J. Mol. Biol. 325, 913-935.


Maluf, N. K., Ali, J. A., and Lohman, T. M. (2003). Kinetic mechanism for formation of the active, dimeric UvrD helicase-DNA complex. J. Biol. Chem. 278, 31930-31940. [free full text]


Maluf, N. K. and Lohman, T. M. (2003). Self-association equilibria of Escherichia coli UvrD helicase studied by analytical ultracentrifugation. J. Mol. Biol. 325, 889-912.


Ali, J. A., Maluf, N. K., and Lohman, T. M. (1999). An oligomeric form of E. coli UvrD is required for optimal helicase activity. J. Mol. Biol. 293, 815-834.


Arakawa, T., Kurosawa, Y., Storms, M., Maruyama, T., Okumura, C. J., and Maluf, N. K. (2016). Biophysical characterization of a model antibody drug conjugate. Drug Discov. Ther. 10, 211-217