Amino Acids


Publication Name:  Current Protocols in Immunology
Unit Number:  Appendix 1B
DOI:  10.1002/0471142735.ima01bs17
Online Posting Date:  May, 2001
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Abstract

The amino acids are listed along with their 3‐letter and 1‐letter codes, molecular weights, accessibility surface area, hydrophobicity, relative mutability and surface probability. The genetic code is also provided.

     
 
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Table of Contents

  • Literature Cited
  • Figures
  • Tables
     
 
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Materials

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Figures

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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.
   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.
   Sweet, R.M. and Eisenberg, D. 1983. Correlation of sequence hydrophobicities measures similarity in three‐dimensional protein structure. J. Mol. Biol. 171:479‐488.
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