Publications
EDUCATION
BS, Brigham Young University (2003)
Ph.D., University of Wisconsin (2008)
NIH Postdoctoral Fellow, The Scripps Research Institute (2008-2011)
PUBLICATIONS
see CV for complete publication list
31. Price, J. L., Smith, M. S., Lawrence, E., Billings, W. M., Larsen, K. S., Bécar, N. A. (2017). An Anion−π Interaction Strongly Stabilizes the β-Sheet Protein WW. ACS Chem. Biol.
30. Price, J. L., Smith, M. S., Billings, W. M., Whitby, F. G., Mille, M. B. (2017). Enhancing a long-range salt bridge with intermediate aromatic and nonpolar amino acids. Organic & Biomolecular Chemistry.
29. Price, J. L., Lawrence, P. B., Billings, W. M., Miller, M. B., Pandey, B. K., Stephens, A. R., Langlois, M. I. (2016). “Conjugation Strategy Strongly Impacts the Conformational Stability of a PEG-Protein Conjugate.”. ACS Chem. Biol., 11, 1805-1809.
28. Price, J. L., Lawrence, P. B. (2016). “How PEGylation Influences Protein Conformational Stability.”. Curr. Opin. Chem. Biol., 34, 88-94.
27. Lawrence, P. B., Gavrilov, Y., Matthews, S. S., Langlois, M. I., Shental-Bechor, D., Greenblatt, H. M., Pandey, B. K., Smith, M. S., Paxman, R., Torgerson, C. D., Merrell, J. P., Ritz, C. C., Prigozhin, M. B., Levy, Y., Price, J. L. (2014). Criteria for Selecting PEGylation Sites on Proteins for Higher Thermodynamic and Proteolytic Stability. J. Am. Chem. Soc., 136, 17547-17560.
26. Pandey, B. K.; Smith, M. S.; Price, J. L.* “Cysi–Lysi+3–Lysi+4 Triad: A General Approach for PEGBased Stabilization of α-Helical Proteins.” Biomacromolecules 2014, ASAP article.
25. Chao, S. -H.; Matthews, S. S.; Paxman, R.; Aksimentiev, A.; Gruebele, M.*; Price, J. L.* “Two Structural Scenarios for Protein Stabilization by PEG.” J. Phys. Chem. B. 2014, 118, 8388–8395.
24. Pandey, B. K.; Enck, S.; Price, J. L.* “Stabilizing Impact of N-Glycosylation on the WW Domain Depends Strongly on the Asn-GlcNAc Linkage.” ACS Chem. Biol. 2013, 8, 2140–2144.
23. Pandey, B. K.; Smith, M. S.; Torgerson, C.; Lawrence, P.B.; Matthews, S. S.; Watkins, E.; Groves, M. L.; Prigozhin, M. B.; Price, J. L.* “Impact of site-specific PEGylation on the conformational stability and folding rate of the Pin WW domain depends strongly on PEG oligomer length.” Bioconjugate Chem. 2013, 24, 796–802. Publications from postdoctoral research at The Scripps Research Institute.
22. Chen, W.; Enck, S.; Price, J. L.; Powers, D. L.; Powers, E. T.; Wong, C. –H.*; Dyson, H. J.*; Kelly, J. W.* “Structural and energetic basis of carbohydrate-aromatic packing interactions in proteins.” J. Am. Chem. Soc. 2013, 135, 9877–9884.
21. Price, J. L.; Culyba, E. K.; Chen, W.; Murray, A. N.; Hanson, S. R.; Wong, C. –H.; Powers, E. T.*; Kelly, J. W.* “N-glycosylation of enhanced aromatic sequons to increase glycoprotein stability.” Peptide Sci. 2012, 98, 195−211.
20. Price, J. L.; Powers, E. T.*; Kelly, J. W.* “N-PEGylation of a Reverse Turn is Stabilizing in Multiple Sequence Contexts unlike N-GlcNAcylation.” ACS Chem. Biol. 2011, 6, 1188–1192.
19. Price, J. L.; Powers, D. L.; Powers, E. T.*; Kelly, J. W.* “Glycosylation of the enhanced aromatic sequon is similarly stabilizing in three distinct reverse turn contexts.” Proc. Natl. Acad. Sci. USA 2011, 108, 14127–14132.
18. Bourgault, S.; Choi, S.; Buxbaum, J. N.; Kelly, J. W.; Price, J. L.; Reixach, N.* “Mechanisms of transthyretin cardiomyocyte toxicity inhibition by resveratrol analogs.” Biochem. Biophys. Res. Commun. 2011, 410, 707–713.
17. Culyba, E. K.; Price, J. L.; Hanson, S. R.; Dhar, A.; Wong, C. –H.; Gruebele, M.; Powers, E. T.*; Kelly, J. W.* “Protein Native State Stabilization by Placing Aromatic Side Chains in N-Glycosylated Reverse Turns.” Science 2011, 331, 571–575. (EKC and JLP share equal authorship) featured in Chemical & Engineering News, February 7, 2011, Vol. 89, pg. 26; and in ScienceBusiness eXchange, February 17, 2011, Vol. 4, doi:10.1038/scibx.2011.184.
16. Price, J. L.; Shental-Bechor, D.; Dhar, A.; Turner, M. J.; Powers, E. T.; Gruebele, M.; Levy; Y.*; Kelly, J. W.* “Context-Dependent Effects of Asparagine Glycosylation on Pin WW Folding Kinetics and Thermodynamics.” J. Am. Chem. Soc. 2010, 132, 15239–15367.
15. Wiseman, R. L.; Zhang, Y.; Lee, K. P. K.; Harding, H. P.; Haynes, C. M.; Price, J.; Sicheri, F.*; Ron, D.* “Flavonol Activation Defines an Unanticipated Ligand-Binding Site in the Kinase-RNase domain of IRE1.” Mol. Cell. 2010, 38, 291–304.
14. Solomon, J. P.; Yonemoto, I. T.; Murray, A. N.; Price, J. L.; Powers, E. T.; Balch, W. E.; Kelly, J. W.* “The 8 and 5 kDa Fragments of Plasma Gelsolin Form Amyloid Fibrils by a Nucleated Polymerization Mechanism, while the 68 kDa Fragment is Not Amyloidogenic.” Biochemistry 2009, 48, 11370–11380. Publications from graduate research at the University of Wisconsin.
13. Price, J. L.; Horne, W. S.; Gellman, S. H.* “Structural Consequences of β-Amino Acid Preorganization in a Self-Assembling α/β-Peptide: Fundamental Studies of Foldameric Helix Bundles.” J. Am. Chem. Soc. 2010, 132, 12378–12387.
12. Price, J. L.; Hadley, E. B.; Steinkruger, J. D.; Gellman, S. H.* “Detection and Analysis of Chimeric Tertiary Structure via Backbone Thioester Exchange: Packing of an α Helix against an α/β-Peptide Helix.” Angew. Chem. Int. Ed. 2010, 49, 368–371.
11. Horne, W. S.; Price, J. L.; Gellman, S. H.* “Interplay among side chain sequence, backbone composition, and residue rigidification in polypeptide folding and assembly.” Proc. Nat. Acad. Sci., USA 2008, 105, 9151–9156.
10. Price, J. L.; Horne, W. S.; Gellman, S. H.* “Discrete Heterogeneous Quaternary Structure Formed by α/β-Peptide Foldamers and α-Peptides.” J. Am. Chem. Soc. 2007, 129, 6376–6377.
9. Horne, W. S.; Price, J. L.; Keck, J. L.; Gellman, S. H.* “Helix Bundle Quaternary Structure from α/β-Peptide Foldamers.” J. Am. Chem. Soc. 2007, 129, 4178–4180.
8. Vollmer-Snarr, H. R.*; Pew, M. R.; Alvarez, M. L.; Cameron, D. J.; Chen, Z.; Walker, G. L.; Price, J. L.; Swallow, J. L. “Amino-Retinoid Compounds in the Human Retinal Pigment Epithelium.” Adv. Exp. Med. Biol. 2006, 572, 69–74.
7. Ziemer, S. P.; Niederhauser, T. L.; Price, J. L.; Woolley, E. M.* “Thermodynamics of proton dissociations from aqueous alanine at temperatures from (278.15 to 393.15) K, molalities from (0.0075 to 1.0) mol · kg−1, and at the pressure 0.35 MPa: Apparent molar heat capacities and apparent molar volumes of alanine, alaninium chloride, and sodium alaninate.” J. Chem. Thermodyn. 2006, 38, 939–951.
6. Ziemer, S. P.; Niederhauser, T. L.; Merkley, E. D.; Price, J. L.; Sorenson, E. C.; McRae, B. R.; Patterson, B. A.; Woolley, E. M.* “Thermodynamics of proton dissociations from aqueous serine at temperatures from (278.15 to 393.15) K, molalities from (0.01 up to 1.0) mol · kg−1, and at the pressure 0.35 MPa: Apparent molar heat capacities and apparent molar volumes of serine, serinium chloride, and sodium serinate.” J. Chem. Thermodyn. 2006, 38, 634–648.
5. Ziemer, S. P.; Niederhauser, T. L.; Merkley, E. D.; Price, J. L.; Sorenson, E. C.; McRae, B. R.; Patterson, B. A.; Origlia-Luster, M. L.; Woolley, E. M.* “Thermodynamics of proton dissociations from aqueous glycine at temperatures from 278.15 to 393.15 K, molalities from 0 to 1.0 mol · kg−1 , and at the pressure 0.35 MPa: Apparent molar heat capacities and apparent molar volumes of glycine, glycinium chloride, and sodium glycinate.” J. Chem. Thermodyn. 2006, 38, 467–483.
4. Price, J. L.; Sorenson, E. C.; Merkley, E. D.; McRae, B. R.; Woolley, E. M.* “Thermodynamics of proton dissociations from aqueous L-valine and L-2-amino-n-butanoic acid: apparent molar volumes and apparent molar heat capacities of the protonated cationic, neutral zwitterionic, and deprotonated anionic species at temperatures from 278.15 ≤ T/K ≤ 393.15, at molalities 0.015 ≤ m/mol · kg−1 ≤ 0.67, and pressure p = 0.35 MPa.” J. Chem. Thermodyn. 2003, 35, 1425–1467.
3. Sorenson, E. C.; Price, J. L.; McRae, B. R.; Woolley, E. M.* “Thermodynamics of proton dissociations from aqueous L-proline: apparent molar volumes and apparent molar heat capacities of the protonated cationic, zwitterionic, and deprotonated anionic forms at temperatures from 278.15 K to 393.15 K and at the pressure 0.35 MPa.” J. Chem. Thermodyn. 2003, 35, 529–553.
2. Origlia-Luster, M. L.; Ballerat-Busserolles, K.; Merkley, E. D.; Price, J. L.; McRae, B. R.; Woolley, E. M.* “Apparent molar volumes and apparent molar heat capacities of aqueous phenol and sodium phenolate at temperatures from 278.15 to 393.15 K and at the pressure 0.35 MPa.” J. Chem. Thermodyn. 2003, 35, 331–347.
1. Price, J. L.; Jardine, J. J.; Call, T. G.; Patterson, B. A.; Origlia-Luster, M. L.; Woolley, E. M.* “Thermodynamics for proton dissociations from aqueous L-histidine at temperatures from 278.15 to 393.15 K and at the pressure 0.35 MPa: apparent molar volumes and apparent molar heat capacities of the protonated cationic, neutral zwitterionic, and deprotonated anionic forms.” J. Chem. Thermodyn. 2003, 35, 195–198.
Dr. Price joined the department faculty June 15, 2011.