Joshua L. Price
Office: C406 BNSN
Office Phone: 801-358-9257
Lab Room: C489 BNSN, C495 BNSN
Lab Phone: 801-422-1199
Email: jlprice@chem.byu.edu
Office Hours
Education:
BS, Brigham Young University (2003)
Ph.D., University of Wisconsin (2008)
NIH Postdoctoral Fellow, The Scripps Research Institute (2008-2011)
Research:
The interests of the Price Research Lab include bioorganic chemistry, protein folding and structure, protein glycosylation's energetic and structural effects, and the design of novel proteins using unnatural amino acids.
Publications:
(See CV for complete list)
42. Stern KL, Dalley NA, McMurray NT, Billings WM, Loftus TJ, Jones ZB, Hadfield JR, Price JL. Prerequisites for Stabilizing Long-Range Synergistic Interactions among b-, c-, and f-Residues in Coiled Coils. Biochemistry. 2022 Mar 1;61(5):319-326. doi: 10.1021/acs.biochem.1c00760. Epub 2022 Feb 7. PubMed PMID: 35129961; PubMed Central PMCID: PMC9202806.
41. Draper SRE, Jones ZB, Earl SO, Dalley NA, Ashton DS, Carter AJ, Conover BM, Price JL. PEGylation Increases the Strength of a Nearby NH-π Hydrogen Bond in the WW Domain. Biochemistry. 2021 Jul 6;60(26):2064-2070. doi: 10.1021/acs.biochem.1c00132. Epub 2021 Jun 17. PubMed PMID: 34137579; PubMed Central PMCID: PMC8406554.
40. Xiao Q, Ashton DS, Jones ZB, Thompson KP, Price JL. Long-range PEG Stapling: Macrocyclization for Increased Protein Conformational Stability and Resistance to Proteolysis. RSC Chem Biol. 2020 Oct 1;1(4):273-280. doi: 10.1039/d0cb00075b. Epub 2020 Aug 13. PubMed PMID: 33796855; PubMed Central PMCID: PMC8009319.
39. Stern KL, Smith MS, Billings WM, Loftus TJ, Conover BM, Della Corte D, Price JL. Context-Dependent Stabilizing Interactions among Solvent-Exposed Residues along the Surface of a Trimeric Helix Bundle. Biochemistry. 2020 May 5;59(17):1672-1679. doi: 10.1021/acs.biochem.0c00045. Epub 2020 Apr 20. PubMed PMID: 32270676; PubMed Central PMCID: PMC8186286.
38. Draper SRE, Ashton DS, Conover BM, Carter AJ, Stern KL, Xiao Q, Price JL. PEGylation near a Patch of Nonpolar Surface Residues Increases the Conformational Stability of the WW Domain. J Org Chem. 2020 Feb 7;85(3):1725-1730. doi: 10.1021/acs.joc.9b02615. Epub 2019 Dec 9. PubMed PMID: 31749365; PubMed Central PMCID: PMC8147659.
37. Xiao Q, Draper SRE, Smith MS, Brown N, Pugmire NAB, Ashton DS, Carter AJ, Lawrence EEK, Price JL. Influence of PEGylation on the Strength of Protein Surface Salt Bridges. ACS Chem Biol. 2019 Jul 19;14(7):1652-1659. doi: 10.1021/acschembio.9b00432. Epub 2019 Jun 24. PubMed PMID: 31188563; PubMed Central PMCID: PMC8147658.
36. Xiao Q, Bécar NA, Brown NP, Smith MS, Stern KL, Draper SRE, Thompson KP, Price JL. Stapling of two PEGylated side chains increases the conformational stability of the WW domain via an entropic effect. Org Biomol Chem. 2018 Nov 28;16(46):8933-8939. doi: 10.1039/c8ob02535e. PubMed PMID: 30444518; PubMed Central PMCID: PMC6290918.
35. Draper SRE, Lawrence PB, Billings WM, Xiao Q, Brown NP, Bécar NA, Matheson DJ, Stephens AR, Price JL. Polyethylene Glycol Based Changes to β-Sheet Protein Conformational and Proteolytic Stability Depend on Conjugation Strategy and Location. Bioconjug Chem. 2017 Oct 18;28(10):2507-2513. doi: 10.1021/acs.bioconjchem.7b00281. Epub 2017 Oct 9. PubMed PMID: 28972368; PubMed Central PMCID: PMC6330093.
34. Kinghorn M, Valdivia-Berroeta G, Chantry D, Smith M, Ence C, Draper S, Duval J, Masino B, Cahoon S, Flansburg R, Conder C, Price J, Michaelis D. Proximity-Induced Reactivity and Product Selectivity with a Rationally Designed Bifunctional Peptide Catalyst. ACS Catalysis. 2017 October; 7(11):7704-7708. doi: 10.1021/acscatal.7b02699.
33. Jalan A, Kastner DW, Webber KGI, Smith MS, Price JL, Castle SL. Bulky Dehydroamino Acids Enhance Proteolytic Stability and Folding in β-Hairpin Peptides. Org Lett. 2017 Oct 6;19(19):5190-5193. doi: 10.1021/acs.orglett.7b02455. Epub 2017 Sep 14. PubMed PMID: 28910115; PubMed Central PMCID: PMC6085080.
32. Jalan A, Kastner DW, Webber KGI, Smith MS, Price JL, Castle SL. Bulky Dehydroamino Acids Enhance Proteolytic Stability and Folding in β-Hairpin Peptides. Org Lett. 2017 Oct 6;19(19):5190-5193. doi: 10.1021/acs.orglett.7b02455. Epub 2017 Sep 14. PubMed PMID: 28910115; PubMed Central PMCID: PMC6085080.
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. Smith MS, Billings WM, Whitby FG, Miller MB, Price JL. Enhancing a long-range salt bridge with intermediate aromatic and nonpolar amino acids. Org Biomol Chem. 2017 Jul 19;15(28):5882-5886. doi: 10.1039/c7ob01198a. PubMed PMID: 28678274.
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. Click here to view article.
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.