Tertiary Structure of Proteins

  • Hans Frauenfelder
Part of the Biological and Medical Physics, Biomedical Engineering book series (BIOMEDICAL)


In Chapter 4, we gave a brief introduction to proteins. The structures of a very large number of proteins have been determined and it is possible to ask fundamental questions: Given the primary sequence, what is tertiary structure? How does the protein fold into the final structure? This “folding problem” has attracted a great deal of attention, and it has become an industry. (One of the Web search engines has more than 106 entries.) We will not treat the folding problem here, but refer to review articles for more information [1]–[7]. Here we discuss a simpler problem, how the main secondary structures, ?-helices and ? pleated sheets , combine to form globular proteins. The folding problem is also treated in Section 17.3.


Tertiary Structure Triose Phosphate Isomerase Polypeptide Backbone Folding Problem Phosphoglycerate Mutase 
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  1. 1.
    F. M. Richards, D. S. Eisenberg, and P. S. Kim. Protein Folding Mechanisms. Academic Press, San Diego, 2000.Google Scholar
  2. 2.
    R. Bonneau and D. Baker. Ab initio protein structure prediction: Progress and prospects. Ann. Rev. Biophys. Biomol. Struct., 30:173–89, 2001.CrossRefGoogle Scholar
  3. 3.
    S. S. Plotkin and J. N. Onuchic. Understanding protein folding with energy landscape theory: Part I: Basic concepts. Q. Rev. Biophys., 35:111–67, 2002.Google Scholar
  4. 4.
    S. S. Plotkin and J. N. Onuchic. Understanding protein folding with energy landscape theory: Part II: Quantitative aspects Q. Rev. Biophys., 35:205-86, 2003.Google Scholar
  5. 5.
    C. Dobson. Principles of protein folding, misfolding, and aggregation. Seminars in Cell and Developmental Biology, 15:3–16, 2004.CrossRefGoogle Scholar
  6. 6.
    J. N. Onuchic and P. G. Wolynes. Theory of protein folding. Curr. Opin. Struct. Bio., 14:70–5, 2004.CrossRefGoogle Scholar
  7. 7.
    M. Oliverberg and P. G. Wolynes. The experimental survey of protein folding energy landscapes. Q. Rev. Biophys., 38:245-86, 2005. Published online June 19, 2006.CrossRefGoogle Scholar
  8. 8.
    C. Chothia, M. Levitt, and D. Richardson. Structure of proteins: packing of alpha-helices and pleated sheets. Proc. Natl. Acad. Sci. USA, 74:4130–4, 1977.CrossRefADSGoogle Scholar
  9. 9.
    D. A. D. Parry and E. N. Baker. Biopolymers. Rep. Progr. Phys., 47:1133–232, 1984.CrossRefADSGoogle Scholar
  10. 10.
    C. Chothia. Principles that determine the structure of proteins. Ann. Rev. Biochem., 53:537–72, 1984.CrossRefGoogle Scholar
  11. 11.
    M. Levitt and C. Chothia. Structural patterns in globular proteins. Nature, 261(5561):552–8, 1976.CrossRefADSGoogle Scholar
  12. 12.
    J. S. Richardson . ? sheet topology and the relatedness of proteins. Nature, 268(5620):495–500, 1977.CrossRefADSGoogle Scholar
  13. 13.
    J. S. Richardson. The anatomy and taxonomy of protein structure. Adv. Protein Chem., 34:167–339, 1981.CrossRefGoogle Scholar

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© Springer Science+Business Media, LLC 2010

Authors and Affiliations

  • Hans Frauenfelder
    • 1
  1. 1.Theory DivisionLos Alamos National LaboratoryLos AlamosUSA

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