Trevor Creamer

Trevor Creamer received the B.S. (with honors) degree in physical and inorganic chemistry and the Ph.D. degree in physical chemistry from the University of Western Australia in 1985 and 1991, respectively. From late 1989 until 1995 he was a postdoctoral scholar training in computational biophysics under the tutelage of Professor George D. Rose. This training was undertaken at the Pennsylvania State University College of Medicine in Hershey, the University of North Carolina, Washington University in St. Louis, and Johns Hopkins University. From 1995 to early 1997, Trevor was a Research Associate at Johns Hopkins University. From 1997 until the present, he has been a member of the faculty in the Department of Molecular and Cellular Biochemistry at the University of Kentucky. Trevor is a founding member of the University of Kentucky Center for Structural Biology, and runs an NSF REU-funded undergraduate summer research program. He is a currently a member of the Biophysical Society Education Committee, 2006—2009, and is inaugural secretary/treasurer, 2007—2009, of the newly formed Intrinsically Disordered Proteins Subgroup of the Biophysical Society. Trevor's research involves using a combination of experimental and computational techniques to study the conformational properties of disordered regions within proteins. These studies include unfolded proteins and more recently intrinsically disordered proteins. He is author of more than thirty peer-reviewed papers and has published a number of book chapters. Trevor is editor of a book titled Unfolded proteins: from denatured to intrinsically disordered to be published in 2008.

Biography Updated on 27 November 2007

Personal Home Page

http://www.mc.uky.edu/Biochemistry/dept_personnel/faculty/creamer.asp

Articles in Scholarly Journals [Incomplete List]

  1. Pressure perturbation calorimetry of helical peptides
    Proteins: Structure, Function, and Bioinformatics, vol. 63, no. 2, pp. 322–326, 2006
  2. Rose is a rose is a rose. Especially if you're a George
    Proteins: Structure, Function, and Bioinformatics, vol. 63, no. 2, pp. 268–272, 2006
  3. Oligoproline Effects on Polyglutamine Conformation and Aggregation
    Journal of Molecular Biology, vol. 355, no. 3, pp. 524–535, 2006
  4. Evidence for Polyproline II Helical Structure in Short Polyglutamine Tracts
    Journal of Molecular Biology, vol. 361, no. 2, pp. 362–371, 2006
  5. Side-chain entropy effects on protein secondary structure formation
    Proteins: Structure, Function, and Bioinformatics, vol. 62, no. 2, pp. 411–420, 2005
  6. Biochemistry, vol. 44, no. 16, pp. 6269–6275, 2005
  7. Biochemistry, vol. 43, no. 19, pp. 5864–5869, 2004
  8. Journal of the American Chemical Society, vol. 126, no. 45, pp. 14734–14735, 2004
  9. Protein simple sequence conservation
    Proteins: Structure, Function, and Bioinformatics, vol. 54, no. 4, pp. 629–638, 2004
  10. Host-guest scale of left-handed polyproline II helix formation
    Proteins: Structure, Function, and Bioinformatics, vol. 53, no. 1, pp. 68–75, 2003
  11. Biochemistry, vol. 42, no. 49, pp. 14690–14695, 2003
  12. Abundance and Distributions of Eukaryote Protein Simple Sequences
    Molecular & Cellular Proteomics, vol. 1, no. 12, pp. 983–995, 2002
  13. Biochemistry, vol. 40, no. 48, pp. 14376–14383, 2001
  14. Side-chain conformational entropy in protein unfolded states
    Proteins: Structure, Function, and Genetics, vol. 40, no. 3, pp. 443–450, 2000
  15. Left-handed polyproline II helix formation is (very) locally driven
    Proteins: Structure, Function, and Genetics, vol. 33, no. 2, pp. 218–226, 1998
  16. Local Interactions in Protein Folding: Lessons from the alpha -Helix
    Journal of Biological Chemistry, vol. 272, no. 3, pp. 1413–1416, 1997
  17. Biochemistry, vol. 36, no. 10, pp. 2832–2835, 1997
  18. Biochemistry, vol. 35, no. 16, pp. 5109–5124, 1996
  19. Direct measurement of salt-bridge solvation energies using a peptide model system: Implications for protein stability
    Proceedings of the National Academy of Sciences, vol. 93, no. 7, pp. 2985–2990, 1996
  20. 1996 Johns Hopkins protein folding meeting
    Proteins: Structure, Function, and Genetics, vol. 25, no. 4, pp. i–iv, 1996
  21. Protein folding: Predicting predicting
    Proteins: Structure, Function, and Genetics, vol. 19, no. 1, pp. 1–3, 1994
  22. a-Helix-forming propensities in peptides and proteins
    Proteins: Structure, Function, and Genetics, vol. 19, no. 2, pp. 85–97, 1994
  23. Macromolecules, vol. 25, no. 3, pp. 1121–1124, 1992
  24. Side-Chain Entropy Opposes  alpha-Helix Formation but Rationalizes Experimentally Determined Helix-Forming Propensities
    Proceedings of the National Academy of Sciences, vol. 89, no. 13, pp. 5937–5941, 1992