Nathan Alder


Associate Professor

University of Connecticut
Department of Molecular & Cell Biology
91 North Eagleville Road, Unit 3125
Biology/Physics Building 207
Storrs, CT 06269-3125

Telephone: 860-486-5154
Fax: 860-486-4331

Visit Assistant Professor Alder’s Website.


Education: Ph.D., University of California, Davis; Postdoctoral study, Texas A&M University

Research Interests: Analysis of the structure, function, and biogenesis of membrane proteins using multiple techniques, primarily fluorescence spectroscopy, and employing yeast as a model system; mitochondrial protein trafficking and assembly; high-resolution fluorescence-based mapping of membrane proteins and analysis of conformational dynamics.

Selected Publications:

Boyd, K.K., Alder, N.N., May, E.R. (2017) Buckling Under Pressure: Curvature Based Lipid Segregation and Stability Modulation in Cardiolipin Containing Bilayers. Langmuir , DOI: 10.1021/acs.langmuir.7b01185

Malhotra, K. and Alder, N.N. (2017) Reconstitution of mitochondrial proteins into nanodiscs by cell-free expression. Methods Mol. Biol. 1567: 155-178.

Sathappa, M., and Alder, N.N. (2016) “The ionization properties of cardiolipin and its variants in model bilayers” BBA-Biomembranes [Epub ahead of print].

Lee, K.K., Imaizumi, N., Chamberland, S.R., Alder, N.N., and Boelsterli, U.A. (2014). Targeting mitochondria with methylene blue protects mice against acetaminophen-induced liver injury. Hepatology. doi: 10.1022/hep.27385.

Hwang, M.S., Schwall C.T., Pazarentzos, E., Datler, C., Alder, N.N., and Grimm, S. (2014). Mitochondrial Ca2+ influx targets cardiolipin to disintegrate respiratory chain complex II for cell death induction. Cell Death Differ. doi: 10.1038/cdd.2014.84 [Epub ahead of print].

Malhotra, K., and Alder, N.N. (2014) Advances in the use of nanoscale bilayers to study membrane protein structure and function. Biotechnol. Genet. Eng. Rev. 30:79-93. doi: 10.1080/02648725.2014.921502.

Malhotra, K., Sathappa, M., Landin, J.S., Johnson, A.E., and Alder, N.N. Structural changes in the mitochondrial Tim23 channel are coupled to the proton-motive force. Nature Structural and Molecular Biology (in press).

Schwall, C.T., and Alder, N.N. Site-specific fluorescent probe labeling of mitochondrial membrane proteins. Methods in Molecular Biology (in press).

Long, A.R., O’Brien, C.C., Malhotra, K., Schwall, C.T., Albert, A.D., Watts, A., and Alder, N.N. (2013). A detergent-free strategy for the reconstitution of active enzyme complexes from native biological membranes into nanoscale discs. BMC Biotechnology 13(1):41 (Epub ahead of print).

Long, A.R., O’Brien, C.C., and Alder, N.N. (2012). The cell-free integration of a polytopic mitochondrial membrane protein into liposomes occurs cotranslationally and in a lipid-dependent manner. PLoS One 7(9): e46332. doi:10.1371/journal.pone.0046332.

Schwall, C.T., Greenwood, V.L., and Alder, N.N. (2012). The stability and activity of respiratory Complex II is cardiolipin-dependent. Biochimica et Biophysica Acta – Bioenergetics 1817, 1588-1596.

Ranaghan, M.J., Schwall, C.T., Alder, N.N., and Birge, R.R. (2011). Green proteorhodopsin reconstituted into nanoscale phospholipid bilayers (nanodiscs) as photoactive monomers. Journal of the American Chemical Society 133, 18318-18327.

Alder, N.N., Jensen, R.E., and Johnson, A.E. (2008). Fluorescence mapping of mitochondrial TIM23 complex reveals a water-facing, substrate-interacting helix surface. Cell 134, 439-450.

Alder, N.N., Sutherland, J., Buhring, A.I., Jensen, R.E., and Johnson, A.E. (2008). Quaternary structure of the mitochondrial TIM23 complex reveals dynamic association between Tim23p and other subunits. Molecular Biology of the Cell 19, 159-170.

Davis, A.J., Alder, N.N., Jensen, R.E., and Johnson, A.E. (2007). The Tim9p/10p and Tim8p/13p complexes bind to specific sites on Tim23p during mitochondrial protein import. Molecular Biology of the Cell 18, 175-486.

Alder, N.N., Shen, Y., Brodsky, J.L., Hendershot, L.M., and Johnson, A.E. (2005). The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum. The Journal of Cell Biology 168, 389-399.

Alder, N.N. and Johnson, A.E. (2004). Cotranslational membrane protein biogenesis at the endoplasmic reticulum. The Journal of Biological Chemistry 279, 22787-22790.

Alder, N.N. and Theg, S.M. (2003). Energy use by biological protein transport pathways. Trends in Biochemical Sciences 28, 442-451.

Alder, N.N. and Theg, S.M. (2003). Energetics of protein transport across biological membranes: a study of the thylakoid ΔpH/cpTat pathway. Cell 112, 231-242.

Alder, N.N. and Theg, S.M. (2003). Protein transport via the cpTat pathway displays cooperativity and is stimulated by transport-incompetent substrate. FEBS Letters 540, 96-100.