People


Dr. Jeff Pelton



email:
jgpelton
at berkeley dot edu
phone: (510) 666-2752
lab: B202A Stanley Hall

NMR Facility
Research Scientist and Resident NMR Superuser

Undergraduate: University of Michigan, Chemical Engineering
PhD: UC Berkeley, Biophysical Chemistry
Staff Fellow: NIH, Bethesda, MD
Research Scientist: LBNL

Research Interests: Application of high field NMR spectroscopy to biological molecules and natural products.

            Publications since 2000 

Hernandez, J.A., Phillips, A.H., Erbil, W.K., Zhao, D., Demuez, M., Zeymer, C., Pelton, J.G., Wemmer, D.E., Rubio, L.M.  (2011) A sterile alpha-motif domain in NafY targets apo-NifDK for iron-molybdenum cofactor delivery via a tethered domain. J. Biol. Chem. 286, p. 6321-6328.

Kim, K.S., Pelton, J.G., Inwood, W.B., Andersen, U., Kustu, S., and Wemmer, D.E. (2010) The Rut pathway for pyrimidine degradation: novel chemistry and toxicity problems.  J. Bacteriol.192, p. 4089-4102.           

Burke, J.R., Deshong, A.J., Pelton, J.G., and Rubin, S.M.  (2010) Phosphorylation-induced conformational changes in the retinoblastoma protein inhibit E2F transactivation domain binding. J. Biol. Chem. 285, p. 16286-16293.

Persil-Cetinkol, O. Dibble, D., Cheng, G., Kent, M.S., Knierim, B., Auer, M. Wemmer, D.E., Pelton, J.G., Melnichenko, Y.B., Ralph, J., Simmons, B.A., and Holmes, B.M. (2010) Understanding the impact of ionic liquid pretreatment on eucalyptus.  Biofuels. 1, 33-46.

Batchelor, J.D., Doucleff, M., Lee, C.J., Matsubara, K., De Carlo, S., Heideker, J., Lamers, M.H., Pelton, J.G., and Wemmer, D.E., (2008). Structure and regulatory mechanism of Aquifex aeolicus NtrC4: variability and evolution in bacterial transcriptional regulation. J Mol Biol 384, p. 1058-75.

Corn, J.E., Pelton, J.G., and Berger, J.M., (2008). Identification of a DNA primase template tracking site redefines the geometry of primer synthesis. Nat Struct Mol Biol 15, p. 163-9.

Doucleff, M., Pelton, J.G., Lee, P.S., Nixon, B.T., and Wemmer, D.E., (2007). Structural basis of DNA recognition by the alternative sigma-factor, sigma54. J Mol Biol 369, p. 1070-8.

Lowery, T.J., Pelton, J.G., Chandonia, J.M., Kim, R., Yokota, H., and Wemmer, D.E., (2007). NMR structure of the N-terminal domain of the replication initiator protein DnaA. J Struct Funct Genomics 8, p. 11-17.

Pirruccello, M., Sondermann, H., Pelton, J.G., Pellicena, P., Hoelz, A., Chernoff, J., Wemmer, D.E., and Kuriyan, J., (2006). A dimeric kinase assembly underlying autophosphorylation in the p21 activated kinases. J Mol Biol 361, p. 312-26.

Roberts, A., Pelton, J.G., and Wemmer, D.E., (2006). Structural studies of MJ1529, an O6-methylguanine-DNA methyltransferase. Magn Reson Chem 44 Spec No, p. S71-82.

Choi, Y.-J., Ryu, K.-S., Ko, Y.-M., YChae, Y.-K., Pelton, J., Wemmer, D.E., and Choi, B.-S., (2005). Biophysical characterization of the interaction domains and mapping of the contact residues in the XPF-ERCC1 complex. J. Biol. Chem. 280, p. 28644-52.

Doucleff, M., Malak, L.T., Pelton, J.G., and Wemmer, D.E., (2005). The C-terminal RpoN domain of sigma54 forms an unpredicted helix-turn-helix motif similar to domains of sigma70. J Biol Chem 280, p. 41530-6.

Nixon, B.T., Yennawar, H.P., Doucleff, M., Pelton, J.G., Wemmer, D.E., Krueger, S., and Kondrashkina, E., (2005). SAS solution structures of the apo and Mg2+/BeF3(-)-bound receiver domain of DctD from Sinorhizobium meliloti. Biochemistry 44, p. 13962-9.

Pelton, J., Shi, J., Yokota, H., Kim, R., and Wemmer, D.E., (2005). NMR structure of hypothetical protein MG354 from Mycoplasma genitalium. Proteins 61, p. 666-668.

Shi, J., Pelton, J.G., Cho, H.S., and Wemmer, D.E., (2004). Protein signal assignments using specific labeling and cell-free synthesis. J Biomol NMR 28, p. 235-47.

Rubin, S.M., Pelton, J.G., Yokota, H., Kim, R., and Wemmer, D.E., (2003). Solution structure of a putative ribosome binding protein from Mycoplasma pneumoniae and comparison to a distant homolog. J Struct Funct Genomics 4, p. 235-43.

Kern, G., Pelton, J., Marqusee, S., and Kern, D., (2002). Structural properties of the histidine-containing loop in HIV-1 RNase H. Biophys Chem 96, p. 285-91.

Cho, H.S., Pelton, J.G., Yan, D., Kustu, S., and Wemmer, D.E., (2001). Phosphoaspartates in bacterial signal transduction. Curr Opin Struct Biol 11, p. 679-84.

Lee, S.Y., Cho, H.S., Pelton, J.G., Yan, D., Berry, E.A., and Wemmer, D.E., (2001). Crystal structure of activated CheY. Comparison with other activated receiver domains. J Biol Chem 276, p. 16425-31.

Lee, S.Y., Cho, H.S., Pelton, J.G., Yan, D., Henderson, R.K., King, D.S., Huang, L., Kustu, S., Berry, E.A., and Wemmer, D.E., (2001). Crystal structure of an activated response regulator bound to its target. Nat Struct Biol 8, p. 52-6.

Stratton, J.R., Pelton, J.G., and Kirsch, J.F., (2001). A novel engineered subtilisin BPN' lacking a low-barrier hydrogen bond in the catalytic triad. Biochemistry 40, p. 10411-6.

Cho, H.S., Lee, S.Y., Yan, D., Pan, X., Parkinson, J.S., Kustu, S., Wemmer, D.E., and Pelton, J.G., (2000). NMR structure of activated CheY. J Mol Biol 297, p. 543-51.

Keating, K.A., Myers, J.D., Pelton, J.G., Bair, R.A., Wemmer, D.E., and Ellis, P.D., (2000). Development and use of a virtual NMR facility. J Magn Reson 143, p. 172-83.