Characteristics of Amino Acids

Andrew Ellington1, J. Michael Cherry1

1 Massachusetts General Hospital, Boston, Massachusetts
Publication Name:  Current Protocols in Molecular Biology
Unit Number:  Appendix 1C
DOI:  10.1002/0471142727.mba01cs33
Online Posting Date:  May, 2001
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Abstract

This appendix presents useful basic information, including common abbreviations, useful measurements and data, characteristics of amino acids and nucleic acids, information on radioactivity and the safe use of radioisotopes and other hazardous chemicals, conversions for centrifuges and rotors, characteristics of common detergents, and common conversion factors.

     
 
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Table of Contents

  • Physical Properties
  • Literature Cited
  • Figures
  • Tables
     
 
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Materials

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Figures

Videos

Literature Cited

Literature Cited
   Chothia, C. 1976. The nature of the accessible and buried surfaces in proteins. J. Mol. Biol. 105:1‐14.
   Dayhoff, M.O., Schwartz, R.M., and Orcutt, B.C. 1978. A model of evolutionary change in proteins. In Atlas of Protein Sequence and Structure (M. Dayhoff, ed.) Vol. 5, pp. 345‐352. National Biomedical Research Foundation, Washington, D.C.
   Frömmel, C. 1984. The apolar surface area of amino acids and its empirical correlation with hydrophobic free energy. J. Theor. Biol. 111:247‐260.
   Rose, G.D., Geselowitz, A.R., Lesser, G.J., Lee, R.H., and Zehfus, M.H. 1985. Hydrophobicity of amino acid residues in globular proteins. Science 229:834‐838.
   Matthew, J.B., Friend, S.H., Botelho, L.H., Lehman, L.D., Hanania, G.I.H., and Gurd, F.R.N. 1979. Biochem. Biophys. Res. Commun. 81:416‐421.
   Sambrook, J., Fritsch, E.F., and Maniatis, T.M. (eds.). 1989. Molecular Cloning: A Laboratory Manual, 2nd ed. Cold Spring Harbor Laboratory Press. Cold Spring Harbor, New York.
   Sharp, P.M., Cowe, E., Higgins, D.G., Shields, D.C., Wolfe, K.H., and Wright, F. 1988. Codon usage patterns in E. coli, B. subtilis, S. cerevisiae, S. pombe, D. melanogaster, and H. sapiens: A review of the considerable within‐species diversity. Nucl. Acids Res. 16:8207‐8211.
   Sweet, R.M. and Eisenberg, D. 1983. Correlation of sequence hydrophobicities measures similarity in three‐dimensional protein structure. J. Mol. Biol. 171:479‐488.
   Wada, K.‐N., Aota, S.‐I., Tsuchiya, R., Ishibashi, F., Gojobori, T., and Ikemura, T. 1990. Codon usage tabulated from the GenBank genetic sequence data. Nucl. Acids Res. 18 (Suppl.): 2367‐2411.
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