Protein Structure

  • Ian M. Rosenberg


Proteins are complex macromolecules made up of successive carboxylic acid—amine residues, amino acids, that are covalently bonded together in a head-to-tail arrangement through substituted amide linkages called peptide bonds. Each protein molecule has a precise length composed of an exact sequence of amino acids which are arranged in a linear, unbranched fashion.


Polypeptide Chain Nonpolar Amino Acid Hydropathy Profile Pleated Sheet Amino Acid Unit 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Alberts B, Bray D, Lewis J, Raff M, Roberts K, Watson JD, eds. (1983): Molecular Biology of the Cell. New York: Garland Publishing, Inc.Google Scholar
  2. Anfinsen CB (1973): Principles that govern the folding of protein chains. Science 181: 223–230CrossRefGoogle Scholar
  3. Cohen FE (1993): The parallel β helix of pectate lyase C: Something to sneeze at. Science 260: 1444–1445CrossRefGoogle Scholar
  4. Degani Y, Degani C (1980): Enzymes with asymmetrically arranged subunits. Trends Biochem Sci 5: 337–341CrossRefGoogle Scholar
  5. Fletterick RJ, Schroer T, Matela RJ, Staples J, eds. (1985): Molecular Structure: Macromolecules in Three Dimensions. Boston: Blackwell Scientific PublicationsGoogle Scholar
  6. Kennelly PJ, Krebs EG (1991): Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases. J Biol Chem 266: 15555–15558Google Scholar
  7. Kyte J, Doolittle RF (1982): A simple method for displaying the hydropathic character of a protein. J Mol Biol 157: 105–132CrossRefGoogle Scholar
  8. Linderstrom-Lang KU, Schellman JA (1959): Protein structure and enzyme activity. In: The Enzymes, Vol.1. Boyer PD, Lardy H, Myrbäck K, eds. New York: Academic PressGoogle Scholar
  9. Monod J, Wyman J, Changeux J-P (1965): On the nature of allosteric transitions: A plausible model. J Mol Biol 12: 88–118CrossRefGoogle Scholar
  10. Morgan RS, Miller SL, McAdon JM (1979): The symmetry of self-complementary surfaces. J Mol Biol 127: 31–39CrossRefGoogle Scholar

General Reference

  1. Creighton TE (1984): Proteins Structures and Molecular Properties. New York: W H Freeman Publishing Co.Google Scholar
  2. Rossmann MG, Argos P (1981): Protein folding. Ann Rev Biochem 50: 497–532CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1996

Authors and Affiliations

  • Ian M. Rosenberg
    • 1
  1. 1.Massachusetts General HospitalBostonUSA

Personalised recommendations