Kathleen Hall, Ph. D.

Kathleen Hall

Biochemistry and Molecular Biophysics

Lab Website
Graduate Programs (DBBS)
Publications (PubMed / NIH)

Office: 2816 North Building
Phone: 314-362-4196
Email: hallkathleen(at)wustl.edu


We study RNA molecules and their interactions with protein partners in order to understand their biology. We use biochemistry, molecular biology, and molecular biophysics to understand the properties of these molecules.

Kathleen Hall's research


  • Hayatshahi H.S., Roe D.R., Galindo-Murillo R., Hall K.B., and Cheatham T.E.
    Computational Assessment of Potassium and Magnesium Ion Binding to a Buried Pocket in the GTPase-Associating Center RNA.
    J Phys Chem B. (2016) (Abstract)

  • Welty R. and Hall K.B.
    Nucleobases Undergo Dynamic Rearrangements during RNA Tertiary Folding.
    J Mol Biol. 428(22):4490-4502 (2016) (Abstract)

  • Bergonzo, C., Hall, K.B and Cheatham, T.E.
    Divalent Ion Dependent Conformational Changes in an RNA Stem-Loop Observed by Molecular Dynamics.
    J Chem Theory Comput. 12:3382-3389 (2016) (Abstract)

  • Bergonzo, C., Hall, K.B. and Cheatham, T.E. Divalent ion dependent conformational changes in an RNA stem-loop observed by molecular dynamics. J Chem Theory Comput. (E-pub ahead of print.) (2016). [Abstract]
  • Bergonzo, C., Hall, K.B. and Cheatham III, T.E. Stem-loop V of Varkud satellite RNA exhibits characteristics of the Mg2+ bound structure in the presence of monovalent ions. J Phys Chem 119:12355-12364 (2015). [Abstract]
  • Rau, M.J., Welty, R., Stump, W.T., and Hall, K.B. Formation of tertiary interactions during rRNA GTPase center folding. J Mol Biol. 427:2799-2815 (2015). [Abstract]
  • Hall, K.B. Mighty tiny. RNA 21:630-631 (2015). [Abstract]
  • Rau, M.J. and Hall, K.B. 2-Aminopurine fluorescence as a probe of local RNA structure and dynamics and global folding. Methods Enzymol. 558:99-124 (2015). [Abstract]
  • Melnykov, A.V., Nayak, R.K., Hall, K.B. and Van Orden, A.K. The effect of loop composition on the stability and folding kinetics of RNA hairpins with large loops. Biochemistry 54:1886-1896 (2015). [Abstract]
  • DeKoster, G.T., Delaney, K.J. and Hall, K.B. A compare-and-contrast NMR dynamics study of two related RRMs: U1A and SNF. Biophys J 107:208-219 (2014). [Abstract]
  • Williams, S.G. and Hall, K.B. Binding affinity and cooperativity control U2B"/snRNA/U2A' RNP formation. Biochemistry 53:3727-3737 (2014). [Abstract]
  • Williams, S.G. and Hall, K.B. Linkage and allostery in snRNP protein:RNA complexes. Biochemistry 53:3529-3539 (2014). [Abstract]
  • Delaney, K.J., Williams, S.G., Lawler, M. and Hall, K.B. Climbing the vertebrate branch of U1A/U2B" protein evolution. RNA 20:1035-1045 (2014). [Abstract]
  • Hall, K.B. Molecular Biology: Protein Binding Cannot Subdue a Lively RNA. Nature 506:303-304 (2014). [Abstract]
  • Hall, K.B. RNA does the folding dance of twist, turn, stack. PNAS 110:16706-16707 (2013). [Abstract]
  • Williams, S.G., Harms, M.J. and Hall, K.B. Resurrection of an Urbilaterian U1A/U2B”/SNF Protein. J Mol Biol 425:3846-3862 (2013). [Abstract]
  • Rau, M., Stump, W.T. and Hall, K.B. Intrinsic flexibility of snRNA hairpin loops facilitates protein binding. RNA 18:1984-1985 (2012). [Abstract]
  • Hall, K.B. Spectroscopic probes of RNA structure and dynamics. Methods Mol Biol 875:67-84 (2012). [Abstract]
  • Nayak, R.K., Peersen, O.B., Hall, K.B. and Van Orden, A.K. Millisecond time scale folding and unfolding of DNA hairpins using rapid-mixing stopped-flow kinetics. J Am Chem Soc (E-pub ahead of print.) (2012). [Abstract]
  • Williams, S.G. and Hall, K.B. Human U2B” protein binding to snRNA stemploops. Biophys Chem 159:82-89 (2011). [Abstract]
  • Williams, S.G. and Hall, K.B. Coevolution of Drosophila snf protein and its snRNA targets. Biochemistry 49:4571-4582. (2010). [Abstract]
  • Liu, F., Maynard, C., Scott, G., Melnykov, A., Hall, K.B. and Gruebele, M. A natural missing link between activated and downhill protein folding scenarios. Phys Chem Chem Phys. 12:3542-3549 (2010). [Abstract]
  • Maynard, C.M. and Hall, K.B. Interactions between PTB RRMs induce slow motions and increase RNA binding affinity. Mol Cell Biol 397:260-277 (2010). [Abstract]