Eighteen publications

  1. George D. Rose, Patrick J. Fleming, Jayanth R. Banavar and Amos Maritan (2006) A backbone-based theory of protein folding. Proc. Nat. Acad. Sci. 103:16623-16633.
  2. Timothy O. Street, D. Wayne Bolen and George D. Rose (2006) A molecular mechanism for osmolyte-induced protein stability. Proc Nat. Acad. Sci. 103: 13997-14002.
  3. Haipeng Gong, Patrick J. Fleming and George D. Rose (2005) Building native protein conformation from highly approximate backbone torsion angles. Proc. Nat. Acad. Sci. 102:16227-16232.
  4. Nicholas C. Fitzkee and George D. Rose (2004) Reassessing random-coil statistics in unfolded proteins. Proc. Nat. Acad. Sci. 101:12497-12502.
  5. Nicholas C. Fitzkee and George D. Rose (2004) Steric restrictions in protein folding: an α-helix cannot be followed by a contiguous β-strand. Protein Science 13: 633-639.
  6. Rajgopal Srinivasan and George D. Rose (2002) Ab initio prediction of protein structure using LINUS, Proteins 47: 489-495.
  7. Rohit V. Pappu, Rajgopal Srinivasan and George D. Rose (2000) The Flory isolated-pair hypothesis is not valid for polypeptide chains: implications for protein folding. Proc Nat. Acad. Sci. 97: 12565-12570.
  8. Rajgopal Srinivasan and George D. Rose (1999) The physical basis of secondary structure in globular proteins. Proc Nat. Acad. Sci. 96: 14258-14263.
  9. Venkatesh L. Murthy, Rajgopal Srinivasan, David E. Draper and George D. Rose (1999) A complete conformational map for RNA. J. Mol. Biol. 291: 313-327.
  10. Rajgopal Srinivasan and George D. Rose (1995) LINUS - A hierarchic procedure to predict the fold of a protein. Proteins: Structure, Function, and Genetics 22: 81-99.
  11. Rajeev Aurora, Rajgopal Srinivasan and George D. Rose (1994) Rules for α-helix termination by glycine. Science 264: 1126-1130.
  12. Edwin T. Harper and George D. Rose (1993) Helix stop signals in proteins and peptides: the capping box. Biochemistry 32: 7605-7609.
  13. Trevor P. Creamer and George D. Rose (1992) Sidechain entropy opposes α-helix formation but rationalizes experimentally-determined helix-forming propensities. Proc. Nat. Acad. Sci., U.S.A. 89: 5937-5941.
  14. Leonard G. Presta and George D. Rose (1988) Helix Signals in Proteins. Science, 240: 1632-1641.
  15. Jacquelyn Leszczynski and George D. Rose (1986) Loops in Globular Proteins. Science 234: 849-855.
  16. George D. Rose, Ari R. Geselowitz, Glenn J. Lesser, Richard H. Lee and Micheal H. Zehfus (1985) Hydrophobicity of Amino Acid Residues in Globular Proteins. Science 229: 834-838.
  17. George D. Rose (1979) Hierarchic Organization of Domains in Globular Proteins. J. Mol. Biol. 134: 447-470.
  18. George D. Rose (1978) Prediction of Chain Turns in Globular Proteins on a Hydrophobic Basis. Nature 272: 586-590.