Publications

Master’s Theses

  • Mead, N. (2024). “Binding studies between HdeA, HdeB and client protein HisJ provide unexpected insights into the mechanism of the acid stress chaperones”
  • Benson, J. (2020). “Investigation of HdeA chaperone action with a native client protein”
  • Geddes-Buehre, D. (2020). “Examination of HdeA mutants to better elucidate the mechanism of acid chaperone activation”
  • Widjaja, M. (2018). “Structure and dynamics studies of the acid-stress chaperone HdeA to investigate its mechanism of activation”
  • Surinarintr, A. (2017). “Investigation of internal motions in TrkB-d5 provides insight into molecular recognition and allostery”
  • Brooks, S. (2016). “Using NMR to probe the role of protein dynamics in interactions between G alpha (i1) and its regulator RGS4”
  • Maly, J. (2013). “The integral role of the SUMO fusion protein system in successful expression and purification of two difficult proteins for NMR studies”
  • Kim, K. (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”
  • Kim, W.H. (2012). “Intermediate timescale exchange in apo TrkB receptor provides insight into the role of molecular motions in its binding selectivity for neurotrophin signaling proteins”
  • Battala, N. (2011). “Development of a protocol to prepare isotopically labeled human neurotrophin-4 (hNT-4) and preliminary characterization of the protein by NMR spectroscopy”
  • Vartanian, T. (2009). “Development of a protocol to express and purify isotopically labelled human Brain Derived Neurotrophic Factor for NMR analysis”

Peer-reviewed (student co-authors in boldface)

  • Nguyen, H.L.D., Crowhurst, K.A. (2024). Solution NMR chemical shift assignment of apo and molybdate-bound ModA at two pHs. Biomol. NMR Assign. 18: 93–98. DOI: 10.1007/s12104-024-10173-7.
  • Aguirre-Cardenas, M.I., Geddes-Buehre, D.H., Crowhurst, K.A. (2021). Removal of disulfide from acid stress chaperone HdeA does not wholly eliminate structure or function at low pH.  Biochem. Biophys. Rep. 27: 101064. DOI: 10.1016/j.bbrep.2021.101064. Open access.
  • Widjaja, M.A., Gomez, J.S., Benson, J.M. & Crowhurst, K.A. (2021). Detection of key sites of dimer dissociation and unfolding initiation during activation of acid-stress chaperone HdeA at low pH. BBA Proteins Proteom. 1869(2): 140576. DOI: 10.1016/j.bbapap.2020.140576. Open access.
  • Pacheco, S., Widjaja, M.A., Gomez, J.S., Crowhurst, K.A. & Abrol, R. (2020). The complex role of the N-terminus and acidic residues of HdeA as pH-dependent switches in its chaperone function. Biophys. Chem. 246: 106406. DOI: 10.1016/j.bpc.2020.106406. Open access.
  • Crowhurst, K.A., Horn, J.V.C. & Weers, P.M.M. (2016). Backbone and side chain chemical shift assignments of apolipophorin III from Galleria mellonella. Biomol. NMR Assign. 10(1):143-147. DOI: 10.1007/s12104-015-9654-7.
    [Abstract] [PDF]
  • Crowhurst, K.A. (2014). 13C, 15N and 1H backbone and side chain chemical shift assignment of acid-stress bacterial chaperone HdeA at pH 6. Biomol. NMR Assign. 8(2): 319-323.
    [Abstract] [PDF]
  • Garrison, M.A. & 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 Sci. 23(2): 167-178.
    [Abstract] [PDF]
  • Maly, J. & Crowhurst, K.A. (2012). Expression, purification and preliminary NMR characterization of isotopically labeled wild-type human heterotrimeric G protein alpha (i1). Prot. Expr. Purif. 84(2): 255-264.
    [Abstract] [PDF]
  • Crowhurst, K.A. & Mayo, S.L. (2008). NMR-detected conformational exchange observed in a computationally designed variant of protein Gß1. Protein Eng. Des. Sel. 21(9): 577-587.
    [Abstract] [PDF]
  • Shah, P.S., Hom, G.K., Ross, S.A., Lassila, J.K., Crowhurst, K.A. & Mayo, S.L. (2007). Full-sequence computational design and solution structure of a thermostable protein variant. J. Mol. Biol. 372(1): 1-6.
    [Abstract] [PDF]
  • Neale, C., Marsh, J.A., Jack, F.E., Choy, W.-Y., Lee, A., Crowhurst, K.A. & 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. J. Mol. Biol. 367(5): 1494-1510.
    [Abstract][PDF]
  • Crowhurst, K.A. & 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.
    [Abstract]
  • Crowhurst, K.A., Choy. W-Y., Mok, Y-K. & 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. J. Mol. Biol. 329(1): 185-187.
    [Abstract] [PDF of published article] [PDF of full-length version]
  • Tollinger, M., Crowhurst, K.A., Kay, L.E. & Forman-Kay, J.D. (2003).  Site-specific contributions to the pH dependence of protein stability. P. Natl. Acad. Sci. USA. 100(8): 4545-4550.
    [Abstract]     [PDF]
  • Crowhurst, K.A., Tollinger, M. & Forman-Kay, J.D. (2002).  Cooperative interactions and a non-native buried Trp in the unfolded state of an SH3 domain.  J. Mol. Biol. 322(1): 163-178.
    [Abstract] [PDF]
  • Choy, W-Y., Mulder, F.A.A, Crowhurst, K.A., Muhandiram, D.R., Millett, I.S., Doniach, S., Forman-Kay, J.D. & 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.  J. Mol. Biol. 316(1): 101-112.
    [Abstract] [PDF]
  • Woolley, G.A., Biggin, P.C., Schultz, A., Lien, L., Jaikaran, D.C.J., Breed, J., Crowhurst, K. & Sansom, M.S.P.  (1997).  Intrinsic rectification of ion flux in alamethicin channels: Studies with an alamethicin dimer.  Biophys. J. 73(2): 770-778.
    [Abstract][PDF]

Posters (student names in boldface)

  • Duguil, D., Martinez A. & Crowhurst, K.A. “Structural and functional impact of conservative alterations to HdeA”. 34th Annual CSU Biotechnology Symposium, held online, January 12-15, 2022.
  • Nguyen, H. & Crowhurst, K.A. “NMR characterization of HdeB chaperone function through its interactions with a client protein ModA”. 34th Annual CSU Biotechnology Symposium, held online, January 12-15, 2022.
  • Hinzer, A. & Crowhurst, K.A. “Investigation of the role of L66 in the internal dynamics of TrkB”. CSUNposium, March 27, 2020.
  • Aguirre-Cardenas, I. & Crowhurst, K.A. “The role of a disulfide bond in the structural plasticity and function of an acid-stress chaperone”. 32nd Annual CSU Biotechnology Symposium, Santa Clara CA, January 16-18, 2020.
  • Geddes-Buehre, D. & Crowhurst, K.A. “Examination of structural HdeA mutants to better elucidate the mechanism of acid chaperone activation”. 32nd Annual CSU Biotechnology Symposium, Santa Clara CA, January 16-18, 2020.
  • Abasi, L. & Crowhurst, K.A. “Use of NMR to probe changes in the flexibility of acid-stress chaperone HdeB from its inactive to active state”. ASBMB Annual Meeting, Orlando FL, April 6-9, 2019.
  • Hinzer, A. & Crowhurst, K.A. “Investigation of Dynamics in hTrkB-d5”. CSUNposium, CSUN campus, April 5, 2019.
  • Geddes-Buehre, D. & Crowhurst, K.A. “Investigation of HdeA mutants to better understand the mechanism of acid chaperone activation”. 31st Annual CSU Biotechnology Symposium, Anaheim CA, January 3-5, 2019.
  • Benson, J.M. & Crowhurst, K.A. “Use of NMR techniques to describe the interactions of the chaperone protein HdeA with its substrate HisJ”. 31st Annual CSU Biotechnology Symposium, Anaheim CA, January 3-5, 2019.
  • Abasi, L. & Crowhurst, K.A. “Use of NMR to probe changes in the flexibility of acid-stress chaperone HdeB from its inactive to active state”. 31st Annual CSU Biotechnology Symposium, Anaheim CA, January 3-5, 2019.
  • Crowhurst, K.A., Widjaja, M. & Gomez, J.S. “NMR characterization of changes in acid-stress bacterial chaperone HdeA as it transitions at low pH to its unfolded and activated state”. XXVIII ICMRBS Meeting, Dublin Ireland, August 18-24, 2018.
  • Crowhurst, K.A., Widjaja, M. & Gomez, J.S. “NMR characterization of changes in acid-stress bacterial chaperone HdeA as it transitions at low pH to its unfolded and activated state”. 32nd Symposium of the Protein Society, Boston MA, July 9-12, 2018.
  • Benson, J.M. & Crowhurst, K.A. “Use of NMR techniques to describe the changes in protein motions of chaperone protein HdeA as a function of pH”. 30th Annual CSU Biotechnology Symposium, Santa Clara CA, January 11-13, 2018.
  • Abasi, L.S. & Crowhurst, K.A. “NMR characterization of chemical shifts and backbone flexibility of chaperone HdeB at pHs 6 and 4.5”. 30th Annual CSU Biotechnology Symposium, Santa Clara CA, January 11-13, 2018.
  • Mahdi, S. & Crowhurst, KA. “Structural and dynamic differences influence the affinities of RGS4 and RGS7 for Gαi1”. Southern California Undergraduate Research Conference, UCLA, April 29, 2017.
  • Mahdi, S. & Crowhurst, K.A. “The investigation of dimerization in human RGS7 using NMR techniques”. CSUNposium, Northridge CA, April 6, 2017.
  • Crowhurst, K.A., Widjaja, M. & Gomez, J.S. “NMR characterization of changes in conformation and dynamics as a function of pH in preparation for activation of acid-stress bacterial chaperone HdeA”. Frontiers of NMR in Life Sciences Keystone Conference, Keystone CO, March 12-17, 2017.
  • Jimenez, J. & Crowhurst, K.A. “Using NMR to probe molecular motions of regulator of G protein signaling 7 (RGS7) in its interactions with Gαi1”. 29th Annual CSU Biotechnology Symposium, Santa Clara CA, January 5-7, 2017.
  • Surinarintr, E. & Crowhurst, K.A. “Localized motions of residues in TrkB-d5 point to a role for dynamics in binding selectivity and allostery”. 29th Annual CSU Biotechnology Symposium, Santa Clara CA, January 5-7, 2017.
  • Widjaja, M. & Crowhurst, K.A. “Use of experimental and computational methods to model increased flexibility and N-terminal structure in the chaperone protein HdeA at pH 2.8”. 29th Annual CSU Biotechnology Symposium, Santa Clara CA, January 5-7, 2017.
  • Mahdi, S. & Crowhurst, K.A. “Comparing the molecular motions of signaling proteins apo RGS7 and RGS4 using NMR”. 28th Annual CSU Biotechnology Symposium, Anaheim CA, January 7-9, 2016.
  • Surinarintr, A. & Crowhurst, K.A. “Novel use of mutagenesis for chemical shift assignment in a very flexible extracellular domain of signaling receptor TrkB”. 28th Annual CSU Biotechnology Symposium, Anaheim CA, January 7-9, 2016.
  • Widjaja, M. & Crowhurst, K.A. “Investigation of Dynamics in Acid-Stress Chaperone Protein HdeA at pH 2.8 using NMR Techniques”. 28th Annual CSU Biotechnology Symposium, Anaheim CA, January 7-9, 2016.
  • Gomez, J. & Crowhurst, K.A. “NMR characterization of the structural properties of acid-stress bacterial chaperone HdeA at pH 2.6, on the cusp of protein unfolding and activation”. 27th Annual CSU Biotechnology Symposium, Santa Clara CA, January 8-10, 2015.
  • Brooks, S.A. & Crowhurst, K.A. “Using NMR to probe the dynamics of binding between Gai1 and Regulator of G protein Signaling 4 (RGS4)”. 27th Annual CSU Biotechnology Symposium, Santa Clara CA, January 8-10, 2015.
  • Simonyan, L., Brooks, S.A. & Crowhurst, K.A. “Evidence for significant changes in backbone conformation and motions between apo and G(alpha)-bound human RGS4”. 28th Symposium of the Protein Society, San Diego CA, July 27-30, 2014.
  • Garrison, M.A. & Crowhurst, K.A. “NMR characterization of the acid stress response of HdeA”. 26th Annual CSU Biotechnology Symposium, Santa Clara CA, January 10-11, 2014.
  • Simonyan, L. & Crowhurst, K.A. “Evidence for backbone motions in human RGS4 provide insight into the potential role of protein flexibility in its interactions with the Ga subunit”. 26th Annual CSU Biotechnology Symposium, Santa Clara CA, January 10-11, 2014.
  • Crowhurst, K.A. & Garrison, M.A. “NMR characterization of the structural and conformational changes triggered by Asp and Glu charge neutralization in preparation for activation of acid-stress bacterial chaperone HdeA”. Gordon Research Conference on Protein Folding Dynamics, Galveston TX, January 5-10, 2014.
  • Maly, J. & Crowhurst, K.A. “Preparation and preliminary NMR characterization of isotopically labeled wild-type human heterotrimeric G protein alphai1”. Keystone Symposium: Frontiers of NMR in Biology, Snowbird UT, January 13-18, 2013.
  • Chaaban, M., Mariduena, N. & Crowhurst, K.A. “Development of a protocol to produce domain 5 of human TrkB with a flexible linker (hTrkB-d5L) and assignment of NMR chemical shifts”. 25th Annual CSU Biotechnology Symposium, Anaheim CA, January 4-5, 2013.
  • Maly, J. & Crowhurst, K.A. “Buffer optimization and NMR analysis of a wild-type human heterotrimeric G protein alpha subunit”. 24th Annual CSU Biotechnology Symposium, Santa Clara CA, January 6-7, 2012.
  • Crowhurst, K.A., Battala, N., Kim, W.H. & Kim, K. “Intermediate protein exchange in apo neurotrophin 4 and its TrkB receptor provide preliminary insight into the role of motions in the binding selectivity of signaling proteins”. 25th Anniversary Symposium of the Protein Society, Boston MA, July 23-27, 2011.
  • Battala, N. & Crowhurst, K. “Preparation of recombinant human Neurotrophin 4 (hNT4) and preliminary characterization by NMR spectroscopy”. 23rd Annual CSU Biotechnology Symposium, Orange County CA, January 7-8, 2011, and the CSUN 15th Annual Student Research & Creative Works Symposium, February 18, 2011.
  • Maly, J. & Crowhurst, K. “Bacterial expression and purification of a wild-type human heterotrimeric G protein alpha subunit for NMR analysis”. 23rd Annual CSU Biotechnology Symposium, Orange County CA, January 7-8, 2011, and the CSUN 15th Annual Student Research & Creative Works Symposium, February 18, 2011.
  • Crowhurst, K. & Kim, W.H. “Preparation of human TrkB domain 5 (hTrkB-d5) and preliminary characterization of its structure and flexibility using heteronuclear NMR”. 24th Annual Symposium of the Protein Society, San Diego CA, August 1-5, 2010.
  • Kim, W.H. & Crowhurst, K. “Expression and purification of recombinant human tropomyosin-related kinase B domain 5 (hTrkBd5) for NMR analysis”. 22nd Annual CSU Biotechnology Symposium, Santa Clara CA, January 8-9, 2010.
  • Schmidt, T. & Crowhurst, K. “Preparation and chemical shift assignment of human RGS7: Progress towards NMR characterization of protein dynamics”. Southern California Undergraduate Research Conference in Chemistry and Biochemistry, USC, Los Angeles CA, April 25, 2009.
  • Vartanian, T & Crowhurst, K. “Expression and purification of human brain-derived neurotrophic factor: Preparation of a 13C/15N labeled sample for NMR analysis”. 21st Annual CSU Biotechnology Symposium, Los Angeles CA, January 16-17, 2009.
  • Vartanian, T. & Crowhurst, K. “Expression and purification of human brain derived neurotrophic factor: Preparation of a 13C/15N labeled sample for NMR analysis”. 22nd Symposium of the Protein Society, San Diego CA, July 19-23, 2008.
  • Crowhurst, K.A. & Mayo, Stephen L. “Dynamics and stability in computationally designed proteins monitored by NMR spectroscopy”. Frontiers in Structural Biology (J6, Keystone Symposia), Keystone CO, Jan 29- Feb 3, 2006.