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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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Unit Introduction
Literature Cited
Figures
Tables

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Figures

Figure A.1B.1

The genetic code. Names of amino acids and chain termination codons are on the periphery of the circle. The first base of the codon is identified in the center ring; the second base of the codon is in the middle ring; and the third base(s) of the codon is in the outer ring of the circle.

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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.