George D. Rose

Krieger-Eisenhower Professor Emeritus and Research Professor.

202 Jenkins Hall
410-516-7244
grose@jhu.edu

Biography
Research
Publications
CV

For a globular protein, function follows form. Under physiological conditions, many proteins undergo a spontaneous disorder ⇌ order transition called folding. Most proteins self-assemble spontaneously in water with a little salt at physiological temperature. The molecular mechanism responsible for this self-organization process remains an open question – perhaps the most fundamental open question in biochemistry.

Protein Folding

folding

Our research is focused primarily on protein folding, the spontaneous disorder ⇌ order transition that occurs under physiological conditions. The protein polymer is flexible when unfolded but adopts its unique native, three dimensional structure when folded. Current experimental knowledge comes primarily from thermodynamic measurements in solution or the structures of individual molecules, elucidated by either X-ray crystallography or NMR spectroscopy. From the former, we know the enthalpy, entropy, and free energy differences between the folded and unfolded forms of hundreds of proteins under a variety of solvent/cosolvent conditions. From the latter, we know the structures of approximately 100,000 proteins, which are built on scaffolds of hydrogen-bonded structural elements, α-helix and β-sheet. Anfinsen showed that the amino acid sequence alone is sufficient to determine a protein’s structure, but the molecular mechanism responsible for self-assembly remains a fundamental open question in chemical biology. ("A backbone-based theory of protein folding" Proc Nat. Acad. Sci. 103: 16623-16633.)

Redrawing the Ramachandran plot

cov1

A protein backbone has two degrees of conformational freedom per residue, described by its φ,ψ‑angles. Accordingly, the energy landscape of a blocked peptide unit can be mapped in two dimensions, as shown by Ramachandran, Sasisekharan and Ramakrishnan almost half a century ago. With atoms approximated as hard spheres, the eponymous Ramachandran plot demonstrated that steric clashes alone eliminate ¾ of φ,ψ‑space, a result that has guided all subsequent work. Here, we show that adding hydrogen-bonding constraints to these steric criteria eliminates another substantial region of φ,ψ‑space for a blocked peptide; for conformers within this region, an amide hydrogen is solvent-inaccessible, depriving it of a hydrogen-bonding partner. Yet, this "forbidden" region is well populated in folded proteins, which can provide longer-range intramolecular hydrogen-bond partners for these otherwise unsatisfied polar groups. Consequently, conformational spaceexpands under folding conditions, a paradigm-shifting realization that prompts an experimentally verifiable conjecture about likely folding pathways. ("Redrawing the Ramachandran plot after inclusion of hydrogen-bonding constraints" Proc. Nat. Acad. Sci., 108:109-113.)

Protein domains - a thermodynamic definition

figure2

Protein domains are conspicuous structural units in globular proteins, and their identification has been a topic of intense biochemical interest dating back to the earliest crystal structures. Numerous disparate domain identification algorithms have been proposed, all involving some combination of visual intuition and/or structure-based decomposition. Instead, we present a rigorous, thermodynamically-based approach that redefines domains as cooperative chain segments. In greater detail, most small proteins fold with high cooperativity, meaning that the equilibrium population is dominated by completely folded and completely unfolded molecules, with a negligible subpopulation of partially folded intermediates. Here, we redefine structural domains in thermodynamic terms as cooperative folding units, based on m-values, which measure the cooperativity of a protein or its substructures. In our analysis, a domain is equated to a contiguous segment of the folded protein whose m‑value is largely unaffected when that segment is excised from its parent structure. Defined in this way, a domain is a self-contained cooperative unit, i.e., its cooperativity depends primarily upon intrasegment interactions, not intersegment interactions. Implementing this concept computationally, the domains in a large representative set of proteins were identified; all exhibit consistency with experimental findings. Specifically, our domain divisions correspond to the experimentally-determined equilibrium folding intermediates in a set of nine proteins. The approach was also proofed against a representative set of 70 additional proteins, again with confirmatory results. Our reframed interpretation of a protein domain transforms an indeterminate structural phenomenon into a quantifiable molecular property grounded in solution thermodynamics. ("A thermodynamic definition of protein domains" Proc. Nat. Acad. Sci., 109: 9420-9425.)

Osmolytes

osmolyte

Osmolytes are small organic compounds that are ubiquitous in living systems. In the equilibrium protein folding reaction, U(nfolded) ⇌ N(ative), protecting osmolytes push the equilibrium toward N while denaturing osmolytes push the equilibrium toward U. As yet, there is no universal molecular theory that can account for the mechanism by which osmolytes interact with the protein backbone to affect protein stability. Here, we lay the groundwork for such a theory, starting with a key observation: the transfer free energy of protein backbone from water to a water:osmolyte solution, ΔGtr, is correlated with an osmolyte’s fractional polar surface area. ΔGtr measures the degree to which an osmolyte stabilizes a protein. Consequently, a straightforward interpretation of this correlation implies that the interaction between the protein backbone and osmolyte polar groups is more favorable than the corresponding interaction with non-polar groups. Such an interpretation immediately suggests the existence of a universal mechanism involving osmolyte, backbone and water. We test this idea by using it to construct a quantitative solvation model in which backbone:solvent interaction energy is a function of interactant polarity, and the number of energetically equivalent ways of realizing a given interaction is a function of interactant surface area. Using this model, calculated ΔGtr values show a strong correlation with measured values (R=0.99). In addition, the model correctly predicts that protecting/denaturing osmolytes will be preferentially excluded/accumulated around the protein backbone. Taken together, these model-based results rationalize the dominant interactions observed in experimental studies of osmolyte-induced protein stabilization and denaturation. ("A molecular mechanism for osmolyte-induced protein stability" Proc Nat. Acad. Sci. 103: 13997-14002.)

  1. Robert L. Baldwin and George D. Rose (2016) How the hydrophobic factor drives protein folding. Proc. Nat. Acad. Sci. 113:12462-12466
  2. George D. Chellapa and George D. Rose (2015) On interpretation of protein X-ray structures: planarity of the peptide unit.Proteins, Structure, Function and Bioinformatics, 83: 1687-1692. [pdf]
  3. Robert L. Baldwin and George D. Rose (2014) Frederic Richards: a NAS biographical memoir. [pdf]
  4. Robert L. Baldwin and George D. Rose (2013) Molten globules, entropy-driven conformational change and protein folding. Curr Opin Struct Biol 23:4-10.
  5. George D. Rose (2013) The open-ended intellectual legacy of GNR in Biomolecular Forms and Function World Scientific Publishing, Singapore
  6. George D. Chellapa and George D. Rose (2012) Reducing the dimensionality of the protein-folding search problem. Protein Science 21:1231-1240.
  7. Lauren L. Porter and George D. Rose (2012) A thermodynamic definition of protein domains. Proc. Nat. Acad. Sci.109:9420-9425.
  8. Laura S. Itzhaki and George D. Rose (2012) Folding and binding: lingering questions, emerging answers. Current Opinion in Structural Biology 22:1-3. [pdf 158K]
  9. Peter Tompa and George D. Rose (2011) The Levinthal paradox of the interactome. Protein Science 20:2074-2079. [pdf 209K]
  10. Lauren L. Porter and George D. Rose (2011) Comment on "Revisiting the Ramachandran plot from a new angle". Protein Science 20:1771-1773 [pdf 285K]
  11. Haipeng Gong, Lauren L. Porter and George D. Rose (2011) Counting peptide-water hydrogen bonds in unfolded proteins. Protein Science 20:417-427. [pdf 1070K]
  12. Lauren L. Porter and George D. Rose (2011) Redrawing the Ramachandran plot after inclusion of hydrogen-bonding constraints. Proc Nat. Acad. Sci. 108:109-113. [pdf 1020K]
  13. Robert L. Baldwin, Carl Frieden and George D. Rose (2010) Dry molten globule intermediates and the mechanism of protein unfolding. Proteins 78:2725-2737. [pdf 284K]
  14. Lauren L. Perskie and George D. Rose (2010) Physical-chemical determinants of coil conformations in globular proteins. Protein Science 19:1127-1136. [pdf 167K]
  15. George D. Rose (2009) In Memoriam: Frederic M. Richards. Proteins 75:535-539. [pdf 214K]
  16. Lauren L. Perskie, Timothy O. Street and George D. Rose (2008) Structures, basins and energies: A deconstruction of the Protein Coil Library. Protein Science 17:1151-1161. [pdf 599K]
  17. D. Wayne Bolen and George D. Rose (2008) Structure and energetics of the hydrogen-bonded backbone in protein folding. Annu. Rev. Biochem. 77:339-362. [pdf 470K]
  18. Haipeng Gong and George D. Rose (2008) Assessing the solvent-dependent surface area of unfolded proteins using an ensemble model. Proc Nat. Acad. Sci. 105:3321-3326. [pdf 516K]
  19. Haipeng Gong, Yang Shen and George D. Rose (2007) Building native protein conformation from NMR backbone chemical shifts using Monte Carlo fragment assembly. Protein Science 16:1515-1521. [pdf 640K]
  20. Timothy O. Street, Nicholas C. Fitzkee, Lauren L. Perskie and George D. Rose (2007) Physical-chemical determinants of turn conformations in globular proteins. Protein Science 16:1720-1727. [pdf 566K]
  21. 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. [pdf 867K]
  22. 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. [pdf 1.3M]
  23. Patrick J. Fleming, Haipeng Gong and George D. Rose (2006) Secondary structure determines protein topology. Protein Science 15:1828-1834. [pdf 393K]
  24. Timothy O. Street, George D. Rose and Doug Barrick (2006) The role of introns in repeat protein gene formation. J. Mol. Biol. 360:258-266. [pdf 588K]
  25. George D. Rose (2006) Lifting the lid on helix-capping. (News and Views) Nature Chemical Biology 2:123-124. [pdf 123K]
  26. 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. [pdf 608K]
  27. Nick Panasik Jr., Patrick J. Fleming and George D. Rose (2005) Hydrogen-bonded turns in proteins: The case for a recount. Protein Science 14:2910-2914. [pdf 189K]
  28. Nicholas C. Fitzkee and George D. Rose (2005) Sterics and solvation winnow accessible conformational space for unfolded proteins. J. Mol. Biol. 353:873-887. [pdf 595K]
  29. Haipeng Gong and George D. Rose (2005) Does secondary structure determine tertiary structure in proteins? Proteins61:338-343. [pdf 179K]
  30. Patrick J. Fleming and George D. Rose (2005) Do all backbone polar groups in proteins form hydrogen bonds? Protein Science 14:1911-1917. [pdf 120K]
  31. Nicholas C. Fitzkee, Patrick J. Fleming and George D. Rose (2005) The Protein Coil Library: A structural database of nonhelix, nonstrand fragments derived from the PDB. Proteins 58:852-854. [pdf]
  32. Nicholas C. Fitzkee, Patrick J. Fleming, Haipeng Gong, Nicholas Panasik Jr, Timothy O. Street and George D. Rose (2005) Are proteins made from a limited parts list? TiBS 30:73-80. [pdf]
  33. Patrick J. Fleming, Nicholas C. Fitzkee, Mihaly Mezei, Rajgopal Srinivasan and George D. Rose (2005) A novel method reveals that solvent water favors polyproline II over β-strand conformation in peptides and unfolded proteins: conditional hydrophobic accessible surface area (CHASA). Protein Science 14:111-118. [pdf 524K]
  34. Patrick J. Fleming and George D. Rose (2005) Conformational Properties of Unfolded Proteins, Protein Folding Handbook, (Eds. Thomas Kiefhaber and Johannes Buchner), Part 1, Vol 2, Chapter 20, pp 710-736, Wiley-VCH (Weinheim). [pdf 282K]
  35. George D. Rose (2005) Secondary structure calculations in protein analysis, Encyclopedia of Biological Chemistry, Academic Press/Elsevier Science.
  36. Nicholas C. Fitzkee and George D. Rose (2004) Reassessing random-coil statistics in unfolded proteins. Proc. Nat. Acad. Sci. 101:12497-12502. [pdf 377K]
  37. Rajgopal Srinivasan, Patrick J. Fleming and George D. Rose (2004) Ab initio protein folding using LINUS. Methods Enzymol. 383:48-66. [pubmed]
  38. Mihaly Mezei, Patrick J. Fleming, Rajgopal Srinivasan and George D. Rose (2004) Polyproline II helix is the preferred conformation for unfolded polyalanine in water. Proteins: Structure, Function and Bioinformatics 55: 502-507. [pdf 291K]
  39. 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. [pdf 286K]
  40. Nancy S. Sung, Jeffrey I. Gordon, George D. Rose, Elizabeth D. Getzoff, Stephen J. Kron, David Mumford, José N. Onuchic, Norbert F. Scherer, DeWitt L. Sumners, and Nancy J. Kopell (2003) Educating future scientists. Science301:1485. [pdf]
  41. Haipeng Gong, Daniel G. Isom, Ragjopal Srinivasan and George D. Rose (2003) Local secondary structure content predicts folding rates for simple two-state proteins. J. Mol. Biol. 327: 1149-1157. [pdf 244K]
  42. Venkatesh L. Murthy and George D. Rose (2003) RNABase: an annotated database of RNA structures. Nucleic Acids Research 31:502-504. [pdf 294K]
  43. Rohit V. Pappu and George D. Rose (2002) A simple model for poly-proline II structure in unfolded states of alanine-based peptides. Protein Science 11:2437-2455. [pdf 466K]
  44. George D. Rose (2002) Getting to know U, in Unfolded Proteins, Advances in Protein Chemistry (G. Rose, ed.) 62:xv-xxi.
  45. Yuan Zhu, Gang Xu, Arun Patel, Megan M. McLaughlin, Carol Solverman, Kristin A. Knecht, Sharon Sweitzer, Ziotong Li, Peter McDonnell, Rosanna Mirabile, Dawn Zimmerman, Rogely Boyce, Lauren A. Tierney, Erding Hu, George P. Livi, Bryan A. Wolf, Sherin S. Abdel-Meguid, George D. Rose, Rajeev Aurora, Preston Hensley, Michael Briggs, and Peter R. Young (2002) Cloning, expression and initial characterization of a novel cytokine-like gene family. Genomics 80: 144-150. [pdf]
  46. Zhengshuang Shi, C. Anders Olson, George D. Rose, Robert L. Baldwin, and Neville R. Kallenbach (2002) Polyproline II structure in a sequence of seven alanine residues. Proc. Nat. Acad. Sci. 99: 9190-9195. [pdf 315K]
  47. Rajgopal Srinivasan and George D. Rose (2002) Methinks it like a folding curve. Biophysical Chemistry 101-102:167-171. [pdf 192K]
  48. Rajgopal Srinivasan and George D. Rose (2002) Ab initio prediction of protein structure using LINUS. Proteins 47: 489-495. [pdf]
  49. Teresa Przytycka, Rajgopal Srinivasan and George D. Rose (2002) Recursive Domains in Proteins. Protein Science 11: 409-417. [pdf 932K]
  50. George D. Rose (2001) Perspective (Remembering Ramachandran). Protein Science 10: 1691-3. [pdf 155K]
  51. Venkatesh L. Murthy and George D. Rose (2000) Is counterion delocalization responsible for collapse in RNA folding? Biochemistry 39: 14365-14370. [pdf 176K]
  52. 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. [pdf 296K]
  53. George D. Rose (2000) Lysozyme among the Lilliputians. Proc Nat. Acad. Sci. 97: 526-528. [pdf 113K]
  54. Rajgopal Srinivasan and George D. Rose (1999) The physical basis of secondary structure in globular proteins. Proc Nat. Acad. Sci. 96: 14258-14263. [pdf 151K]
  55. 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. [pdf 818K]
  56. Huimin Xu, Rajeev Aurora, George D. Rose, and Robert H. White (1999) Identifying two ancient enzymes in Archaea. Nature Structural Biology 6: 750-754 [pdf 486K]
  57. Teresa Przytycka, Rajeev Aurora, George D. Rose (1999) A Protein Taxonomy Based on Secondary Structure. Nature Structural Biology 6: 672-682. [pdf 2M]
  58. Robert L. Baldwin and George D. Rose (1999) Is protein folding hierarchic? II. Folding Intermediates and Transition States. Tibs 24: 77-83. [pdf 485K]
  59. Robert L. Baldwin and George D. Rose (1999) Is protein folding hierarchic? I. Local Structure and Peptide Folding. Tibs24: 26-33. [pdf 223K]
  60. Rajeev Aurora and George D. Rose (1998) Helix capping, Protein Science 7: 21-38.
  61. Rajeev Aurora and George D. Rose (1998) Seeking an Ancient Enzyme in Methanococcus jannaschii using ORF, a Program Based on Predicted Secondary Structure Comparisons, Proc. Nat. Acad. Sci. 95: 2818-2823.
  62. Rose, George D. (1997) Protein Folding and the Paracelsus Challenge (News and Views), Nature Structural Biology 4: 512-514.
  63. Trevor P. Creamer, Rajgopal Srinivasan and George D. Rose (1997) Modeling unfolded states of peptides and proteins. II. Backbone solvent accessibility. Biochemistry 36: 2832-2835.
  64. Rajeev Aurora, Trevor P. Creamer, Rajgopal Srinivasan, and George D. Rose (1997) Local interactions in protein folding: lessons from the a-helix J. Biol. Chem. 272: 1413-1416.
  65. George D. Rose (1996) No assembly required. The Sciences, 36: 26-31.
  66. Trevor P. Creamer, Rajgopal Srinivasan and George D. Rose (1995) Modeling unfolded states of peptides and proteins.Biochemistry 34: 16245-16250.
  67. George D. Rose, Rajeev Aurora and Rajgopal Srinivasan (1995) Possible exceptions to rules for a-helix termination by glycine. Science 269: 1451-1452. [Technical Comments]
  68. William L. Nichols, George D. Rose, Lynn F. Ten Eyck and Bruno H. Zimm (1995) Rigid domains in proteins: an algorithmic approach to their identification. Proteins: Structure, Function, and Genetics 23: 38-48.
  69. Trevor P. Creamer and George D. Rose (1995) Interactions between hydrophobic side chains within a-helices. Protein Science 4: 1305-1314.
  70. Trevor P. Creamer and George D. Rose (1995) Simple Forcefield for Study of Peptide and Protein Conformational Properties. Methods in Enzymology 259: 576-589.
  71. 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.
  72. Trevor P. Creamer, Rajgopal Srinivasan and George D. Rose (1995) Evaluation of Interactions between residues in a-helices by Exhaustive Conformational Search. Techniques in Protein Chemistry VI, ed. John Crabb, Academic Press, San Diego, pages 443-450.
  73. Rajgopal Srinivasan and George D. Rose (1994) The T → R transformation in hemoglobin; a reevaluation, Proc. Nat. Acad. Sci. 91: 11113-11117.
  74. Jeffrey W. Seale, Rajgopal Srinivasan, and George D. Rose (1994) Sequence determinants of the capping box, a stabilizing motif at the N-termini of a-helices. Protein Science 3: 1741‑1745.
  75. Laura Lin, Rachel J. Pinker, Kirk Forde, George D. Rose and Neville R. Kallenbach (1994) Molten globular characteristics of the native state of apomyoglobin. Nature, Structural Biology 1: 447-452.
  76. Rajeev Aurora, Rajgopal Srinivasan and George D. Rose (1994) Rules for α-helix termination by glycine. Science 264: 1126-1130.
  77. George D. Rose and Trevor P. Creamer (1994) Protein folding: Predicting predicting. Proteins: Structure, Function, and Genetics 19: 1-3.
  78. Trevor P. Creamer and George D. Rose (1994) α-helix-forming propensities in proteins and peptides. Proteins: Structure, Function, and Genetics 19: 85-97.
  79. Edwin T. Harper and George D. Rose (1993) Helix stop signals in proteins and peptides: the capping box. Biochemistry32: 7605-7609.
  80. Rachel J. Pinker, Laura Lin, George D. Rose and Neville R. Kallenbach (1993) Effects of alanine substitutions in α-helices of sperm whale myoglobin on protein stability. Protein Science 2: 1099-1105.
  81. George D. Rose and Richard Wolfenden (1993) Hydrogen bonding, the hydrophobic effect, packing, and protein folding. Ann. Rev. Biophysics and Biological Structure 22: 381-415.
  82. Eaton E. Lattman and George D. Rose (1993) Protein folding – what’s the question? Proc. Nat. Acad. Sci. 90: 439-441.
  83. Douglas F. Stickle, Leonard G. Presta, Ken A. Dill and George D. Rose (1992) Hydrogen bonding in globular proteins. J. Mol. Biol. 226: 1143-1159.
  84. Trevor P. Creamer and George D. Rose (1992) Sidechain entropy opposes a-helix formation but rationalizes experimentally-determined helix-forming propensities. Proc. Nat. Acad. Sci. 89: 5937-5941.
  85. George D. Rose (1991) Preface to Conformations and Forces in Protein Folding, eds. Barry T. Nall and Ken A. Dill, vii-viii, American Association for the Advancement of Science, Washington, D.C.
  86. Michael J. Behe, Eaton E. Lattman and George D. Rose (1991) Protein folding: the native fold determines packing, but does packing determine the native fold? Proc. Nat. Acad. Sci., 88: 4195-4199.
  87. Glenn J. Lesser and George D. Rose (1990) Hydrophobicity of amino acid subgroups in proteins. PROTEINS: Structure, Function, and Genetics 8: 6-13.
  88. George D. Rose (1990) Structural Themes in Protein Folding: Deciphering the Second Half of the Genetic Code, eds. Lila Gierash and Jonathan King, 1-3, American Association for the Advancement of Science, Washington, D.C.
  89. George D. Rose and Jonathan E. Dworkin (1989) The Hydrophobicity Profile in Prediction of Protein Structure and the Principles of Protein Conformation, ed. G. Fasman, 625-633, Plenum Pub. Corp., New York.
  90. J.S. Fetrow, F. Sherman and George D. Rose (1989) Deletion and replacement of omega loops in iso-1-cytochrome c from the yeast Saccharomyces cerevisiae. Proceedings of Biotech USA, 327-336.
  91. George D. Rose (1988) Hydrophobicity Profiles, Computational Molecular Biology, ed. A.M. Lesk, 198-204, Oxford University Press, Oxford.
  92. Leonard G. Presta and George D. Rose (1988) Helix Signals in Proteins. Science 240: 1632-1641.
  93. Jacquelyn Fetrow, Micheal H. Zehfus and George D. Rose (1988) Protein Folding: New Twists. Bio/Technology 6: 167-171.
  94. George D. Rose (1987) Protein Hydrophobicity: Is It The Sum of Its Parts? PROTEINS: Structure, Function, and Genetics 2: 79-80.
  95. Jonathan E. Dworkin and George D. Rose (1987) Hydrophobicity Profiles Revisited. Methods in Protein Sequence Analysis-1986, K.A. Walsh, ed., pgs. 573-586, Humana Press, Clifton, NJ.
  96. John A. Smith and George D. Rose (1987) Immune Recognitions of Proteins: Conclusions, Dilemmas, and Enigmas.Bioessays 6: 112-116.
  97. Glenn J. Lesser, Richard H. Lee, Micheal H. Zehfus and George D. Rose (1987) Hydrophobic Interactions in Proteins, Protein Engineering: Tutorials in Molecular and Cell Biology, 175-179, Alan R. Liss, New York.
  98. Jacquelyn Leszczynski and George D. Rose (1986) Loops in Globular Proteins. Science 234: 849-855.
  99. Micheal H. Zehfus and George D. Rose (1986) Compact Units in Proteins. Biochemistry 25: 5759-5765.
  100. David W. Fanning, John A. Smith and George D. Rose (1986) Molecular Cartography of Globular Proteins with Application to Antigenic Sites. Biopolymers 25: 863-883.
  101. George D. Rose and Richard H. Lee (1986) Molecular Recognition in Macromolecules. Biophys. J. 49: 83-85.
  102. Jiri H. Novotny, Mark Schumacher, Edgar Haber, Robert E. Bruccoleri, William B. Carlson, David W. Fanning, John A. Smith and George D. Rose (1986) Antigenic Determinants in Proteins Coincide with Surface Regions Accessible to Large Probes (Antibody Domains). Proc. Natl. Acad. Sci. 83: 226-230.
  103. David W. Fanning, John A. Smith and George D. Rose (1985) Algorithmic Identification of Antigenic Determinants in Proteins of Known Structure, Peptides: Structure and Function. Proc. 9th American Peptide Symposium, pgs. 13-22, C.M. Deber, V.J. Hruby, and F.D. Kopple, eds. Pierce Chemical Co., Rockford, IL.
  104. Micheal Zehfus, Jack P.. Seltzer and George D. Rose (1985) Fast Approximations for Accessible Surface Area and Molecular Volume in Protein Segments. Biopolymers 24: 2511-2518.al Co., Rockford, IL.
  105. 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.
  106. Richard H. Lee and George D. Rose (1985) Molecular Recognition I. Automatic Identification of Topographic Surface Features. Biopolymers 24: 1613-1627.
  107. George D. Rose (1985) Automatic Identification of Domains in Globular Proteins. Methods in Enzymology, Academic Press, New York. 115: 430-440.
  108. George D. Rose, Lila Gierasch and John A. Smith (1985) Turns in Peptides and Proteins. Advances in Protein Chemistry, Academic Press, New York. 37: 1-109.
  109. Jeffrey E. Lacy, Lila M. Gierasch, Arlene L. Rockwell and George D. Rose (1983) Reverse Turns in Hydrophobic Environments, Peptides: Structure and Function. Proc. 8th American Peptide Symposium, 781-784, V. Hruby and D.H. Rich, eds. Pierce Chemical Co., Rockford, IL.
  110. George D. Rose, William B. Young and Lila M. Gierasch (1983) Interior Turns in Globular Proteins. Nature 304: 654-657.
  111. Thomas J. Yuschok and George D. Rose (1983) Hierarchic Organization of Globular Proteins: A Control Study. Int. J. Peptide Protein Res. 21: 479-484.
  112. Arthur M. Lesk and George D. Rose (1981) Folding Units in Globular Proteins. Proc. Nat. Acad. Sci. 78: 4304-4308.
  113. George D. Rose (1980) A Hierarchic Model for the Self-Assembly of Globular Proteins. Biophysical J. 32: 419-422.
  114. George D. Rose and Siddhartha Roy (1980) The Hydrophobic Basis of Packing in Folded Proteins. Proc. Nat. Acad. Sci.77: 4643-4647.
  115. Donald B. Wetlaufer and George D. Rose (1980) Modular Assembly of Proteins. Proc. Int. Symp. Biomolecular Structure, Conformation, Function and Evolution, Pergamon Press, London.
  116. George D. Rose (1979) Hierarchic Organization of Domains in Globular Proteins. J. Mol. Biol. 134: 447-470.
  117. George D. Rose (1978) Prediction of Chain Turns in Globular Proteins on a Hydrophobic Basis. Nature 272: 586-590.
  118. George D. Rose and Donald B. Wetlaufer (1977) The Number of Turns in Globular Proteins. Nature 268: 769-770.
  119. George D. Rose and Jack Seltzer (1977) A New Algorithm for Finding the Peptide Chain Turns in a Globular Protein. J. Mol. Biol. 113: 153-164.
  120. Donald B. Wetlaufer, George D. Rose and L. Taaffe (1976) Orientation of Structural Segments in Globular Proteins.Biochemistry 15: 5154-5157.
  121. George D. Rose, Ronald H. Winters and Donald B. Wetlaufer (1976) A Testable Model for Protein Folding. FEBS Letters63: 10-16.
  122. D. Goldberg, S. Saliterman and D.B. Wetlaufer, in collaboration with G.D. Rose and T. Hopkins (1975) Minimization of Construction Errors in Bent Wire Protein Models. Biopolymers 14: 633-640.

Education

  • 1976 Oregon State University, Ph.D. (Biochemistry and Biophysics) K.E. Van Holde, advisor
  • 1972 Oregon State University, M.S. (Mathematics and Computer Science)
  • 1963 Bard College, B.S. (Mathematics)

Professional Experience

  • 2014- Research Professor and Krieger-Eisenhower Professor Emeritus, Dept. of Biophysics, Krieger School of Arts and Sciences, Johns Hopkins University, Baltimore, MD 21218 (Joint appointment: Professor, Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205)
  • 2002-14 Krieger-Eisenhower Professor and Chair (2004-2007), Dept. of Biophysics, Krieger School of Arts and Sciences, Johns Hopkins University, Baltimore, MD 21218 (Joint appointment: Professor, Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205)
  • 1994-02 Professor, Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205 (Joint appointment, 1997‑02: Professor, Department of Biophysics, Krieger School of Arts and Sciences, Johns Hopkins University, Baltimore, MD 21218 .)
  • 1992-94 Alumni Endowed Professor of Biochemistry and Molecular Biophysics (Professor, 1992‑3), Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110
  • 1991-92 Professor, Department of Biochemistry and Biophysics; Adjunct Professor, Department of Chemistry, University of North Carolina, Chapel Hill, NC 27599-7260.
  • 1980-91 Distinguished Professor (Chairman 1988-89; Professor 1986-89; Associate Professor 1980-86), Department of Biological Chemistry, The M.S. Hershey Medical Center, The Pennsylvania State University, Hershey, PA 17033
  • 1975-80 Assistant Professor, Assistant Research Professor, Senior Research Associate, Chemistry Department, University of Delaware, Newark, DE 19711
  • 1967-75 Assistant-to-Director, Research Associate, Manager, Operating Systems and Systems Programming, Oregon State University Computer Center,Corvallis, OR 97331
  • 1966-67 Member of the Technical Staff, Auerbach Corporation, Philadelphia, PA
  • 1963-66 Associate Research Scientist, Director Laboratory on Communication Sciences, New York University Medical School, Department of Neurology, New York, NY 10036

Grants Fellowships and Honors

  • 2014 Temporary Eminent Scholar, Faculty of the Technische Universität München, Dept. Chemistry
  • 2011 Honorary Hans Fischer Senior Fellow, Institute for Advanced Study, Technische Universität München
  • 2011 Humboldt Research Award (Forschungspreise)
  • 2010 Exceptional Lecturer, Feinberg Teaching Survey, Weizmann Institute Student and Fellows Council
  • 2008 Elected to Oregon State University Academy of Distinguished Engineers
  • 2005 Elected Fellow of the American Association for the Advancement of Science (AAAS)
  • 2004 Krieger-Eisenhower Professor, Johns Hopkins University
  • 2002 Fellow of the John Simon Guggenheim Memorial Foundation
  • 1999 John and Samuel Bard Award in Medicine and Science, Bard College
  • 1985 Hinkle Award & Lectureship, Hinkle Society of Pennsylvania State University
  • 1980-85 National Institutes of Health Research Career Development Award (AG-00088)
  • 1966-69 Honorary Associate in Computer and Information Sciences, American Museum of Natural History, NYC
  • 2010-17 National Science Foundation, Protein Domains
  • 1999-15 G. Harold and Leila Y. Mathers Charitable Foundation, Integrative Biology
  • 1990-09 Program in Molecular and Computational Biophysics (Training grant) (Co-I)
  • 1979-05 NIH GM-29458 Self-recognition in Globular Proteins
  • 1996-01 NIH GM-51362 Structural/Thermodynamic Studies of Folding and Binding
  • 1999-07 Burroughs Wellcome Fund Program: Interfaces Program
  • 1991-93 NIH GM-41484 Stability of Native and Altered Proteins
  • 1985-89 NIH AG-06084 Stability of Native and Altered Proteins