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Robert Newberry, PhD

TitlePostdoctoral Scholar
SchoolUCSF School of Pharmacy
DepartmentPharmaceutical Chemistry
Address555 Mission Bay Blvd South
San Francisco CA 94158
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    Collapse Biography 
    Collapse Education and Training
    University of Wisconsin-MadisonPhD2016Chemistry
    The University of Texas at AustinBS2011Biochemistry
    The University of Texas at AustinBA2011Liberal Arts
    Collapse Awards and Honors
    University of California, San Francisco2016  - 2017Institutional Research Service Award
    University of Wisconsin-Madison2014  - 2015Division of Organic Chemistry Graduate Fellowship, American Chemical Society
    University of Wisconsin-Madison2012  - 2014Biotechnology Training Program Fellowship

    Collapse Overview 
    Collapse Overview
    I am broadly interested in how the intrinsic, chemical properties and features of proteins bias them toward specific structures, particularly the amyloid state implicated in many neurodegenerative disorders. My work integrates approaches and perspectives from the fields of biophysics and chemical biology to dissect the determinants of folding and misfolding in proteins linked to human diseases like Alzheimer's or Parkinson's. Understanding what makes proteins susceptible or resistant to misfolding will inform strategies for targeted intervention.


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    Collapse Publications
    Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Researchers can login to make corrections and additions, or contact us for help.
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    1. Newberry R, Raines RT. The n→π* Interaction. Acc Chem Res. 2017 Aug 15; 50(8):1838-1846. PMID: 28735540.
      View in: PubMed
    2. Newberry R, Raines RT. A prevalent intraresidue hydrogen bond stabilizes proteins. Nat Chem Biol. 2016 Oct 17. PMID: 27748749.
      View in: PubMed
    3. Newberry R, Orke SJ, Raines RT, et al. n?p* Interactions Are Competitive with Hydrogen Bonds. Org Lett. 2016 Jul 13. PMID: 27409515.
      View in: PubMed
    4. Newberry R, Raines RT. 4-Fluoroprolines: Conformational Analysis and Effects on the Stability and Folding of Peptides and Proteins. Top Heterocycl Chem. 2017; 48:1-25. PMID: 28690684.
      View in: PubMed
    5. Newberry R, VanVeller B, Raines RT. Thioamides in the collagen triple helix. Chem Commun (Camb). 2015 Jun 14; 51(47):9624-7. PMID: 25967743; PMCID: PMC4449287 [Available on 05/28/16].
      View in: PubMed, PubMed Central
    6. Choudhary A, Newberry R, Raines RT. n?p* interactions engender chirality in carbonyl groups. Org Lett. 2014 Jul 3; 16(13):3421-3. PMID: 24926562; PMCID: PMC4096190.
      View in: PubMed, PubMed Central
    7. Newberry R, Bartlett GJ, VanVeller B, Woolfson DN, Raines RT. Signatures of n?p* interactions in proteins. Protein Sci. 2014 Mar; 23(3):284-8. PMID: 24375625; PMCID: PMC3945836.
      View in: PubMed, PubMed Central
    8. Newberry R, Raines RT. A key n?p* Interaction in N-acyl homoserine lactones. ACS Chem Biol. 2014 Apr 18; 9(4):880-3. PMID: 24556113; PMCID: PMC4219647.
      View in: PubMed, PubMed Central
    9. Bartlett GJ, Newberry R, VanVeller B, Raines RT, Woolfson DN. Interplay of hydrogen bonds and n?p* interactions in proteins. J Am Chem Soc. 2013 Dec 11; 135(49):18682-8. PMID: 24256417; PMCID: PMC3940535.
      View in: PubMed, PubMed Central
    10. Newberry R, Raines RT. n?p* interactions in poly(lactic acid) suggest a role in protein folding. Chem Commun (Camb). 2013 Sep 11; 49(70):7699-701. PMID: 23897514; PMCID: PMC3839959.
      View in: PubMed, PubMed Central
    11. Newberry R, VanVeller B, Guzei IA, Raines RT. n?p* interactions of amides and thioamides: implications for protein stability. J Am Chem Soc. 2013 May 29; 135(21):7843-6. PMID: 23663100; PMCID: PMC3742804.
      View in: PubMed, PubMed Central
    12. Ragain CM, Newberry R, Ritchie AW, Webb LJ. Role of electrostatics in differential binding of RalGDS to Rap mutations E30D and K31E investigated by vibrational spectroscopy of thiocyanate probes. J Phys Chem B. 2012 Aug 9; 116(31):9326-36. PMID: 22738401.
      View in: PubMed
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