Barrick Lab

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Barrick Lab
216 Jenkins Hall
3400 N. Charles Street
Baltimore, MD 21218

(410) 516-0409 office
(410) 516-4118 fax

       

Selected Publications
  • Lubman, O.Y., Ilagan, M.X.G., Kopan, R., & Barrick, D. (2007) Quantitative Dissection of the Notch:CSL Interaction: Insights into the Notch Transcriptional Switch. J. Mol. Biol. 365, 577-589.
  • Bradley, C.M. & Barrick, D. (2006) The Notch Ankyrin Domain Folds Through a Discrete, Centralized Pathway. Structure 14, 1303-1312.
  • Street, T.O., Rose, G.D., & Barrick, D. (2006) The Role of Introns in Repeat-Protein Gene Formation. J. Mol. Biol. 360, 258-266.
  • Zweifel, M.E., Leahy, D.J., & Barrick, D. (2005) Structure and Notch-receptor binding of the tandem WWE domain of Deltex. Structure 13, 1599-1611.
  • Mello, C., Bradley, C.M., Tripp, K.W., & Barrick, D. (2005) Experimental Characterization of the Folding Kinetics of the Notch Ankyrin Domain. J. Mol. Biol. 352, 266-281.
  • Street, T.O., Bradley, C.M., & Barrick, D. (2005) An improved experimental system for measuring small folding entropy changes resulting from proline-->alanine substitutions. Prot. Sci. 14, 2129-2135.
  • Mello, C., & Barrick, D. (2004) An experimentally determined protein folding energy landscape. Proc. Natl. Acad. Sci. USA 101, 14102-14107.
  • Bertanga, A.M. & Barrick, D. (2004) Nonspecific hydrophobic interactions stabilize an equilibrium intermediate of apomyoglobin at a key position within the AGH region. Proc. Natl. Acad. Sci USA 101,  12514-12519.
  • Zweifel, M.E., Leahy, D.J., Hughson, F.M., & Barrick, D. (2003) Structure and stability of the ankyrin domain  
  • Barrick, D. & Hughson, F.M. (2002) Irreversible assembly of membrane fusion machines [News & Views], Nature Structural Biology 9, 78-80.
  • Zweifel, M. E., & Barrick, D. (2001) Studies of the ankyrin repeats of the Drosophila melanogaster Notch receptor: I.  Solution conformational and hydrodynamic properties.  Biochemistry 40, 14344-14356.
  • Zweifel, M. E., & Barrick, D. (2001) Studies of the ankyrin repeats of the Drosophila melanogaster Notch receptor: II.  Solution stability and folding cooperativity.  Biochemistry 40, 14357-14367.
  • Barrick, D., Ho, N. T., Simplaceanu, V., & Ho C. (2001) Distal ligand reactivity and quaternary structure studies of proximally detached hemoglobins.  Biochemistry 40, 3780-3795.
  • Barrick, D. 2000. Studies of the proximal ligand hydrogen bond in myoglobin using in trans ligand substitution. II. Energetics, functional consequences, and implications for hemoglobin allostery. Proteins: Struc. Funct. Genet. 39:291-308.
  • Barrick, D., and F.W. Dahlquist. 2000. Studies of the proximal ligand hydrogen bond in myoglobin using in trans ligand substitution. I. Structural and spectroscopic consequences of hydrogen bond deletion. Proteins: Struc. Funct. Genet. 39:278-290.
  • Barrick, D., N.T. Ho, V. Simplaceanu, F.W. Dahlquist, and C. Ho. 1997. Molecular signaling in hemoglobin: A test of the Perutz model for cooperativity. Nat. Struct. Biol. 4:78-83.
  • Scholtz, J.M., D. Barrick, E.J. York, J.M. Stewart, and R.L. Baldwin. 1995. Urea unfolding of peptide helices as a model for interpreting protein unfolding. Proc. Natl. Acad. Sci. USA 92:185-189.
  • Barrick, D. 1995. Depletion and replacement of protein metal ligands. Curr. Opin. Biotechnol. 6:411-418.
  • Barrick, D. 1994. Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His-93->Gly. Biochemistry 33:6546-6554.
  • Barrick, D., K. Villanueba, J. Childs, R. Kalil, T.D. Schneider, C.E. Lawrence, L. Gold, and G.D. Stormo. 1994. Quantitative analysis of ribosome binding sites in E. coli. Nucleic Acids Res. 22:1287-1295.
  • Barrick, D., F.M. Hughson, and R.L. Baldwin. 1994. Molecular mechanisms of acid denaturation: The role of histidine residues in the partial unfolding of apolyoglobin. J. Mol. Biol. 237:588-601.
  • Barrick, D., and R.L. Baldwin. 1993. A three-state analysis of apomyoglobin unfolding. Biochemistry 32:3790-3796.
  • Hughson, F.M., D. Barrick, and R.L. Baldwin. 1991. Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis. Biochemistry 30:4113-4118.
  • Childs, J., Villanueba, K., Barrick, D., Schneider, T., Stormo, G., Gold, L., Leitner, M., & Caruthers, M. (1985) Ribosome binding site sequences and function.  In Sequence Specificity in Transcription and Translation..  Calender, R., and Gold, L., (eds.) New York, New York: Alan R. Liss, 341-350.