Skip Navigation
Johns Hopkins University logoProgram in Molecular Biophysics
Kalina HristovaHristova Lab

Kalina Hristova

Department of Materials Science and Engineering
Whiting School of Engineering

B.S. 1987, University of Sofia, Bulgaria
M.S. 1988, University of Sofia, Bulgaria
Ph.D. 1994, Duke University

Croft Hall 204 H
3400 N. Charles Street
Baltimore, MD 21218

Office: 410-516-8939
Lab: 410-516-7142


School of Engineering logo

Membranes and membrane proteins are abundant in eukaryotic cells. About 30% of all human proteins are expected to be membrane-associated. The pharmacological importance of membrane proteins is determined by the role they play in vital processes such as cell adhesion, recognition, motility, proliferation, energy production, transport of nutrients and cholesterol, and cell signaling. Despite their functional importance and abundance, it is not yet clear how the majority of these proteins function at the molecular level, and how the membrane shapes protein function.

We use diverse biophysical and cell biological methods such as X-ray and neutron diffraction, fluorescence, Western blotting, circular dichroism, equilibrium dialysis, and molecular modeling to address questions such as:

  • What structural and thermodynamic laws govern membrane protein folding (and pathogenic misfolding)?
  • How do mutations in the transmembrane segments of catalytic receptors induce pathological phenotypes such as cancers and growth disorders?
  • Can we, through structural and kinetic studies of membrane proteins, arrive at a “recipe” for the rational design of drugs that inhibit persistent membrane protein activation?
  • How does the lipid bilayer mediate protein-protein interactions?

Selected Publications

Sarabipour, S., and K. Hristova. (2013) FGFR3 transmembrane domain interactions persist in the presence of its extracellular domain. Biophys. J. 105:165-71.

Cruz, J., M. Mihailescu, G. Wiedman, K. Herman, P.S. Searson, W.C.Wimley, and K. Hristova. (2013) A membrane-translocating peptide penetrates into bilayers without significant bilayer perturbations. (2013) Biophys. J. 104:2419-28 (Highlighted by the Editor).

Sarabipour, S., and K. Hristova. (2013) Glycophorin A transmembrane domain dimerization in plasma membrane vesicles derived from CHO, HEK 293T, and A431 cells. Biochim. Biophys. Acta- Biomembranes 1828:1829-33.

Chen, F., S. Sarabipour, and K. Hristova. (2013) Multiple consequences of a single amino acid pathogenic RTK mutation: the A391E mutation in FGFR3. PloS One 8:e56521.

Wiedman, G., K. Herman, P.S. Searson, W.C.Wimley and K. Hristova. (2013) The electrical response of bilayers to the bee venom toxin melittin: evidence for transient bilayer permeabilization. Biochim. Biophys. Acta- Biomembranes, 1828:1357-1364.

He, L., and K. Hristova. (2012) Consequences of replacing EGFR juxtamembrane domain with an unstructured sequence. Sci. Rep. 2:854.

Placone, J., and K. Hristova. (2012) Direct assessment of the effect of the Gly380Arg achondroplasia mutation on FGFR3 dimerization using quantitative imaging FRET. PloS One 7:e46678.

Del Piccolo, N., J. Placone, L. He, S.C. Agudelo, and K. Hristova. (2012) Production of plasma membrane vesicles with chloride salts and their utility as a cell membrane mimetic for biophysical characterization of membrane protein interactions. Anal. Chem. 28:6088-96.

He, J., K. Hristova, and W.C.Wimley. (2012) A highly charged voltage-sensor helix spontaneously translocates across membranes. Angew. Chem. Int. Ed. Engl. 51:7150-7153.

He, L., C. Serrano, N. Niphadkar, N. Shobnam, and K. Hristova. (2012) Effect of the G375C and G346E achondroplasia mutations on FGFR3 activation. PloS One 7:e34808.

Lin, J., J. Motylinki, A.J. Krauson, W.C. Wimley, P. Searson, and K. Hristova. (2012) Interactions of membrane active peptides with planar supported bilayers: an impedance spectroscopy study. Langmuir 28:6088-96.

Stahl, P.J., J.C. Cruz, Y. Li, M.S. Yu, and K. Hristova. (2012) On-the-resin N-terminal modification of long synthetic peptides. Anal. Biochem. 424:137-139.

He, L., and K. Hristova. (2011) Physical-chemical principles underlying RTK activation, and their implications for human disease. Biochim. Biophys. Acta- Biomembranes (in press)

Li, E., W.C. Wimley, and K. Hristova. (2011) Transmembrane helix dimerization: Beyond the search for sequencxe motifs. Biochim. Biophys. Acta- Biomembranes 1818:183-193.

Chen, F., and K. Hristova. (2011) The physical basis of FGFR3 response to fgf1 and fgf2. Biochemistry 50:8576-8582.

He, L., A. Hoffmann, C. Serrano, K. Hristova, and W.C. Wimley. (2011) High-throughput selection of transmembrane sequences that enhance receptor tyrosince kinase activation. J. Mol. Biol. 412:43-54.

Marks, J., J. Placone, K. Hristova, and W.C. Wimley. (2011) Spontaneous membrane-translocating peptides by orthogonal high-throughput screening. J. Am. Chem. Soc. 133:8995-9004.

Chen, F., C. Degnin, M. Laedrich, W.A. Horton, and K. Hristova. (2011) The A391E mutation enhances FGFR3 activation in the absence of ligand. Biochim. Biophys. Acta- Biomembranes 1808:2045-2050.

He, L., N. Shobnam, W.C. Wimley, and K. Hristova. (2011) FGFR3 heterodimerization in achondroplasia, the most common form of human dwarfism. J. Biol. Chem. 286:13272-13281.

Wimley, W.C., and K. Hristova. (2011) Antimicrobial peptides: Successes, challenges, and unanswered questions. J. Membr. Biol. 239:27-34.

Hristova, K., and W.C. Wimley. (2011) A look at arginine in membranes. J. Membr. Biol. 239:49-56.

He, L., N. Shobnam, and K. Hristova. (2011) Specific inhibition of a pathogenic receptor tyrosine kinase by its transmembrane domain. Biochim. Biophys. Acta- Biomembranes 1808:253-259.

Chen, L., J. Placone, L. Novicky, and K. Hristova. (2010) The extracellular domain of fibroblast growth factor receptor 3 inhibits ligand-independent dimerization. Science Signaling 3:ra86.

© 2008 The Johns Hopkins University. All rights reserved.