Dept. of Chemistry & Biochemistry

18111 Nordhoff Street
Northridge, California 91330-8262

Phone: (818) 677-3381
Fax: (818) 677-4068

Office: 2102 Eucalyptus Hall

Hours: Mon-Fri 8:00am-5:00pm

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Karin Crowhurst

Karin Crowhurst


Department of Chemistry and Biochemistry
California State University, Northridge
Northridge, California, 91330-8262

telephone: (818) 677-4288
fax: (818) 677-4068

e-mail: Karin.Crowhurst at

office: 3109 Citrus Hall


  • Ph.D., (Biochemistry) University of Toronto, 2003
  • M.Sc., (Chemistry) University of Toronto, 1997
  • B.Sc., Honours (Chemistry) Queen's University, 1995


  • California Institute of Technology, 2003-2006


  • Chemistry 100,   Principles of Chemistry
  • Chemistry 461L, Biochemistry I laboratory
  • Chemistry 462L, Biochemistry II laboratory
  • Chemistry 464,   Principles of Biochemistry
  • Chemistry 464L, Principles of Biochemistry laboratory
  • Chemistry 465,   Topics in Biochemistry
  • Chemistry 595P, Investigating Protein Structure and Function



Dr. Crowhurst’s research is focused generally on using multidimensional, multinuclear NMR spectroscopy to better understand the mechanisms of signal transduction in the brain. In particular, we are interested in understanding the roles of structure, biophysical properties and protein dynamics in the specificity and affinity of interactions between proteins and their targets involved in several signaling cascades.

We are focusing specifically on two different families of proteins: neurotrophins and RGS proteins. The neurotrophin family of proteins is responsible for providing the signal for the growth and differentiation of neurons in the brain. These proteins also have an important influence on synaptic function, learning and memory. Members of the RGS protein family are responsible for turning off a common type of signaling cascade in the brain. Ultimately, RGS proteins control the relay of signals that are triggered by light, smell, hormones or neurotransmitters. We would like to understand how proteins in both families bind to their specific targets (and avoid other targets that are only slightly different) and how changes in protein structure help in transmitting signals. Since both of these protein families are critical for the initiation or regulation of signaling cascades, answers to questions may lead to an increased understanding of the mechanisms that cause conditions such as cerebral stroke, chronic pain, cancer, epilepsy, depression, schizophrenia and neurodegenerative diseases (such as Alzheimer’s and Parkinson’s diseases) and can aid in the design of drugs to treat these conditions.

The protein NMR spectroscopic techniques applied by the lab to address these biological questions are, by necessity, more sophisticated and provide significantly more information than one can obtain through recording the standard one-dimensional 1H or 13C spectra. Our experiments will require the recording of 2D and 3D spectra, in which the signals of multiple nuclei are linked to each other to provide detailed information about structural and dynamic properties of proteins.

Students joining the lab will have the opportunity to expand their understanding of the mechanism and biophysical properties of signaling proteins at a detailed, molecular level. In addition, they can gain experience in expressing and purifying isotopically labeled proteins, in running multidimensional NMR experiments and in using specialized computer software to analyze the collected data and obtain information about protein structure and motions.



  1. Garrison, M.A. and Crowhurst, K. A. (2014) "NMR-monitored titration of acid-stress bacterial chaperone HdeA reveals that Asp and Glu charge neutralization produces a loosened dimer structure in preparation for protein unfolding and chaperone activation” Protein Science, 23(2), 167-178. DOI: 10.1002/pro.2402

  2. Crowhurst, K. A. (2013) "13C, 15N and 1H backbone and side chain chemical shift assignment of acid-stress bacterial chaperone HdeA at pH 6” Biomolecular NMR Assignments, available online. DOI:10.1007/s12104-013-9508-0

  3. Maly, J. and Crowhurst, K. A. (2012) "Expression, purification and preliminary NMR characterization of isotopically labeled wild-type human heterotrimeric G protein α(i1)” Protein Expression and Purification, 84(2), 255-264.

  4. Crowhurst, K. A. and Mayo, S. L. (2008) "NMR-detected conformational exchange observed in a computationally designed variant of protein Gβ1” Protein Engineering, Design and Selection 21(9), 577-587.

  5. Shah, P. S., Hom, G. K., Ross, S. A., Lassila, J. K., Crowhurst, K. A. and Mayo, S. L. (2007) “Full-sequence computational design and solution structure of a thermostable protein variant,” Journal of Molecular Biology 372(1), 1-6.

  6. Neale, C., Marsh, J. A., Jack, F. E., Choy, W.-Y., Lee, A., Crowhurst, K. A. and Forman-Kay, J. D. (2007) “Improved structural characterization of the drkN SH3 domain unfolded state suggest a compact ensemble with native-like and non-native structure” Journal of Molecular Biology 367(5), 1494-1510.

  7. Crowhurst, K. A. and Forman-Kay, J. D. (2003) “Aromatic and methyl NOEs point to hydrophobic clustering in the unfolded state of an SH3 domain” Biochemistry-US 42(29), 8687-8695.

  8. Crowhurst, K. A., Choy. W-Y., Mok, Y-K. and Forman-Kay, J. D. (2003) “Corrigendum to the paper by Mok et al. (1999) NOE data demonstrating a compact unfolded state for an SH3 domain under non-denaturing conditions” Journal of Molecular Biology 329(1), 185-187.

  9. Tollinger, M., Crowhurst, K. A., Kay, L. E. and Forman-Kay, J. D. (2003) “Site-specific contributions to the pH dependence of protein stability” Proceedings of the National Academy of Sciences USA. 100(8), 4545-4550.

  10. Crowhurst, K. A., Tollinger, M. and Forman-Kay, J. D. (2002) “Cooperative interactions and a non-native buried Trp in the unfolded state of an SH3 domain” Journal of Molecular Biology. 322(1), 163-178.

  11. Choy, W-Y., Mulder, F. A. A, Crowhurst, K. A., Muhandiram, D. R., Millett, I. S., Doniach, S., Forman-Kay, J. D. and Kay, L. E. (2002) “Distribution of molecular size within an unfolded state ensemble using small-angle X-ray scattering and pulse field gradient NMR techniques” Journal of Molecular Biology 316(1), 101-112.


  • "The integral role of the SUMO fusion protein system in successful expression and purification of two difficult proteins for NMR studies"
    Jan Maly (MS Biochemistry 2013)


  • "Expression and purification trials of human brain-derived neurotrophic factor (hBDNF) and its cognate receptor, tropomyosin-related kinase B (hTrkB), to characterize their conformational dynamics by NMR spectroscopy"
    Keen Kim (MS Biochemistry 2013)


    "Intermediate timescale exchange in apo TrkB receptor provides insight into the role of molecular motions in its binding selectivity for neurotrophin signaling proteins"
    William H. Kim (MS Biochemistry 2012)


    "Development of a protocol to prepare isotopically labeled human neurotrophin-4 (hNT-4) and preliminary characterization of the protein by NMR spectroscopy"
    Naveen Battala (MS Biochemistry 2011)


    "Development of a protocol to express and purify isotopically labelled human Brain Derived Neurotrophic Factor for NMR analysis"
    Tamara Vartanian (MS Biochemistry 2009)