Associate Professor
Department of Materials Science and Engineering
Whiting School of Engineering

hristova@jhu.edu

101F Maryland Hall
3400 N. Charles Street
Baltimore, MD 21218

Office: 410-516-8939

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 methods such as X-ray and neutron diffraction, fluorescence, 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
Merzlyakov, M., L. Chen, and K. Hristova. (2007) Studies of receptor tyrosine kinase transmembrane domain dimerization: The EmEx-FRET method. J. Membr. Biol. 215:93-103.

Hristova, K. (2006) Book Review: Lipid Rafts and Caveolae: From Membrane Biophysics to Cell Biology, edited by C. J. Fielding. ChemBioChem. 7:1279-1280.

Merzlyakov, M., E. Li, I. Gitsov, and K. Hristova. (2006) Surface-supported bilayers with transmembrane helices: The role of the polymer cushion revisited. Langmuir 22:10145-10151.

Han, X., and K. Hristova. (2006) Neutron diffraction studies of fluid bilayers with transmembrane proteins: Structural consequences of the achondroplasia mutation. Biophys. J. 91:3736-3747.

Merzlyakov, M., E. Li, R. Casas, and K. Hristova. (2006) Spectral FRET detection of protein interactions in surface supported bilayers. Langmuir 22:6986-6992.

Li, E., M. You, and K. Hristova. (2006) FGFR3 Dimer stabilization due to a single amino acid pathogenic mutation. J. Mol. Biol. 356:600-612.

Merzlyakov, M., E. Li, and K. Hristova. (2006) Directed Assembly of surface-supported bilayers with transmembrane helices. Langmuir 22:1247-1253.

Merzlyakov, M., M. You, E. Li, and K. Hristova. (2006) Transmembrane helix heterodimerization in lipid bilayers: probing the energetics behind autosomal dominant growth disorders. J. Mol. Biol. 358:1-7.

You, M., E. Li, and K. Hristova. (2006) The achondroplasia mutation does not alter the dimerization energetics of FGFR3 transmembrane domain. Biochemistry 45:5551-5556.

Li, E., and K. Hristova. (2006) Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies. Biochemistry 45:6241-6251.

Iwamoto, T., M. You, E. Li, J. Spangler, J.M. Tomich, and K. Hristova. (2005) Synthesis and initial characterization of FGFR3 transmembrane domain: Consequences of sequence modifications. BBA-Biomembranes. 1668:240-247.

You, M., E. Li, W.C. Wimley, and K. Hristova. (2005) FRET in liposomes: Measurements of transmembrane helix dimerization in the native bilayer environment. Anal. Biochem. 340:154-164.

Li, E., M. You, and K. Hristova. (2005) SDS-PAGE and FRET suggest weak interactions between FGFR3 TM domains in the absence of extracellular domains and ligands. Biochemistry 44:352-360.

Hristova, K., and S.H. White (2005) An experiment-based algorithm for predicting the partitioning of unfolded peptides into phosphatidylcholine bilayer interfaces. Biochemistry 44:12614-12619.

Li, E., and K. Hristova. (2004) Imaging FRET measurements of transmembrane helix interactions in lipid bilayers on a solid support. Langmuir 20:9053-9060.