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Proteins

  • J. Stenesh

Abstract

In the first half of the 19th century, the Dutch chemist Gerardus Mulder was investigating the properties of substances extractable from both animal and plant tissues. He found these to contain carbon, hydrogen, nitrogen, and oxygen and believed them to be “without doubt the most important of the known substances in living matter, and without them life would be impossible on our planet.” In 1838, at the suggestion of the Swedish chemist Ws Jakob Berzelius, Mulder named these substances “proteins” (from the Greek, meaning “first” or “foremost”).

Keywords

Disulfide Bond Polypeptide Chain Peptide Bond Globular Protein Cyanogen Bromide 
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.

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Selected Readings

  1. Borman, S., Scientists refine understanding of protein folding and design, Chem. Eng. News, May 27, 1996.Google Scholar
  2. Bradley, W. A., Gianturco, S. H., and Segrest, J. P. (eds.), Plasma lipoproteins, Part C, Methods in Enzymology, Vol. 263, Academic Press, San Diego (1996).Google Scholar
  3. Creighton, T. E., Proteins—Structures and Molecular Properties, 2nd ed., W. H. Freeman, New York (1993).Google Scholar
  4. Doolittle, R. F., The multiplicity of domains in proteins, Annu. Rev. Biochem. 64: 287–314 (1995).PubMedCrossRefGoogle Scholar
  5. Dreuth, J., Principles of Protein X-Ray Crystallography, Springer-Verlag, New York (1994).CrossRefGoogle Scholar
  6. Eaton, W. A., and Hofrichter, J., Sickle cell hemoglobin polymerization, Adv. Protein Chem. 40: 63–279 (1988).CrossRefGoogle Scholar
  7. Eisenberg, D. S., and Richards, F. M., Protein stability, Adv. Protein Chem. 46: 1–311 (1995).CrossRefGoogle Scholar
  8. Huang, C. S., He, W., Meister, A., and Anderson, M. E., Amino acid sequence of rat kidney glutathione synthetase, Proc. Natl. Acad. Sci. USA 92: 1232–1236 (1995).PubMedCrossRefGoogle Scholar
  9. Karger, B. L., and Hancock, W. S. (eds.), High resolution separation and analysis of biological macromolecules, Part B, Methods in Enzymology, Vol. 271, Academic Press, San Diego (1996).Google Scholar
  10. Liu, Y., Van Heeswijck, R., Hj, P., and Hoogenraad, N., Purification and characterization of omithine acetyltransferase from Saccharomyces cerevisiae, Eur. J. Biochem. 228: 291–296 (1995).Google Scholar
  11. Olson, J. S., and Phillips, G. N., Jr., Kinetic pathways and barriers for ligand binding to myoglobin, J. Biol. Chem. 271: 17593–17596 (1996).PubMedCrossRefGoogle Scholar
  12. Ozols, J., Amino acid analysis, in Methods in Enzymology, Vol. 182, pp. 587–601, Academic Press, San Diego (1990).Google Scholar
  13. Pain, R. H. (ed.), Mechanisms of Protein Folding, IRL Press, Oxford (1994).Google Scholar
  14. Pauling, L, Corey, R. B., and Branson, H. R., The structure of proteins: Two hydrogen-bonded helical configurations of the polypeptide chains, Proc. Natl. Acad. Sci. USA 37: 205–211 (1951).PubMedCrossRefGoogle Scholar
  15. Perutz, M. F., Mechanisms of Cooperativity and Allosteric Regulation in Proteins, Cambridge University Press, Cambridge (1990).Google Scholar

Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • J. Stenesh
    • 1
  1. 1.Western Michigan UniversityKalamazooUSA

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