Overview of the Physical State of Proteins within Cells

Howard R. Petty1

1 Wayne State University, Detroit
Publication Name:  Current Protocols in Protein Science
Unit Number:  Unit 1.5
DOI:  10.1002/0471140864.ps0105s31
Online Posting Date:  May, 2003
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Abstract

To understand how proteins work it is necessary to understand their physical state within the cell. This unit reviews the classification of proteins, how that is related to the hydropathicity of the protein, other factors that affect the heterogeneity of proteins, protein assemblies, methods for altering the solubility of proteins, and limitations of in vitro manipulations of proteins.

     
 
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Table of Contents

  • Protein Classifications
  • Hydropathy Patterns Often Reflect a Protein's Classification
  • Membrane Proteins
  • Additional Factors Affecting the Physical Heterogeneity of Proteins
  • Protein Assemblies
  • Altering the Solubility of Proteins: Protein Extraction
  • Limitations of the In Vitro Manipulation of Proteins
  • Conclusions
  • Figures
  • Tables
     
 
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Materials

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Figures

Videos

Literature Cited

Literature Cited
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   Cardoso de Almeida, M.L. 1992. GPI Membrane Anchors. Academic Press, New York.
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   Freedman, R.B. and Hawkins, H.C. 1980. The Enzymology of Post‐Translational Modifications of Proteins,Vol. 1. Academic Press, New York.
   Freedman, R.B. and Hawkins, H.C. 1985. The Enzymology of Post‐Translational Modifications of Proteins,Vol. 2. Academic Press, New York.
   Hoppe‐Seyler, F. 1864. Über die chemischen und optischen Eigenschaften des Blutfarbstoffs. Virchows Arch. 29:233‐235.
   Hubbard, S.R., Wei, L., Ellis, L., and Hendrickson, W.A. 1994. Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature. 372:746‐754.
   Kühn, W. 1876. Über das Verhalten verschiedner organisirter und sogenannter ungeformter Fermete. Über das Trypsin (Enzym des Pankreas) [Reprint, FEBS Lett. 62:E3‐E7 (1976).]
   Kyte, J. and Doolittle, R.F. 1982. A simple method for displaying the hydrophobic character of a protein. J. Mol. Biol. 157:105‐132.
   Parry, D.A.D. 1987. Fibrous protein structure and sequence analysis. In Fibrous Protein Structure (J.M. Squire and P.J. Vibert eds.) pp. 141‐171. Academic Press, New York.
   Petty, H.R. 1993. Molecular Biology of Membranes:Structure and Function. Plenum,New York.
   Petty, H.R., Worth, R.G., and Todd, R.F. III. 2002. Interactions of integrins with their partner proteins in leukocyte membranes. Immunol. Res. 25:75‐95.
   Racker, E. 1985. Reconstitutions of Transporters, Receptors, and Pathological States. Academic Press, New York.
   Rietveld, A. and Simons, K. 1998. The differential miscibility of lipids as the basis for the formation of functional membrane rafts. Biochim. Biophys. Acta. 1376:467‐479.
   Schlesinger, M.J., Magee, A.I., and Schmidt, M.F.G. 1980. Fatty acylation of proteins in cultured cells. J. Biol. Chem. 255:10021‐10024.
   Schultz, G.E. and Schirmer, R.M. 1979. Principles of Protein Structure. Springer‐Verlag, New York.
   Spiess, M. 1995. Heads or tails—what determines the orientation of proteins in the membrane. FEBS Lett. 369:76‐79.
   Squire, J.M. and Vibert, P.J.(eds.) 1987. Fibrous Protein Structure. Academic Press, New York.
   von Heijne, G. and Gavel, Y. 1988. Topogenic signals in integral membrane proteins. Eur. J. Biochem. 174:671‐678.
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Key References
   Racker, 1985. See above.
  A wonderful little book on membrane protein manipulation which disproves the hypothesis that scientists can't write.
   Tanford, C. 1961. Physical Chemistry of Macromolecules. Academic Press, New York.
  A rigorous introduction to the physical properties of proteins, which remains useful several decades later.
   Tanford, C. 1980. The Hydrophobic Effect. John Wiley & Sons, New York.
  A very readable introduction to the hydrophobic effect.
Internet Resources
  http://www.expasy.ch
  A user‐friendly protein database including two‐dimensional PAGE data and 3D protein structures.
  ftp://ftp.pdb.bnl.gov/
  Contains protein crystallography data.
  http://www.ncbi.nlm.nih.gov
  An important protein database.
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