Bacteriophage Cytochrome c Oxidase Click on molecules for description DNA Polymerase Myoglobin
Molecules and descriptions are from PDB

Bioinformatics and Computational Molecular Biology

Algorithms and Hardware

The Amino Acids

 

With few exceptions, proteins are composed of the following set of 20 amino acids. These amino acids are also sometimes call residues. Each amino acid has a full name, a three-letter code, and a one-letter code. The one-letter code is what is stored in most protein sequence databases. There are also some special one-letter codes which might appear in the database if the amino acid at a particular location is not fully known.

Click on the picture of any amino acid to get a RasMol file for interactive viewing. These files are in PDB format, so save the file with a *.pdb extension before opening with RasMol.

Alpha Carbon atom = pink

Hydrogen = orange (shown only in glycine - omitted in the others)

Other Carbon atoms = grey

Nitrogen = blue

Sulfur = yellow

Oxygen = red

In the schmatic diagrams the main-chain atoms are in pink and the side-chain atoms are in black.

 

In a Class by Itself:

Glycine, Gly, G

Hydrophobic (water hating) Amino Acids:

Alanine, Ala, A

Valine, Val, V

Phenylalanine, Phe, F

Proline, Pro, P (the N atom is in the main chain - proline is the only case where a main chain N is shown)

Methionine, Met, M

Isoleucine, Ile, I

Leucine, Leu, L

Hydrophilic (water loving) Amino Acids:

Serine, Ser, S

Threonine, Thr, T

Tyrosine, Tyr, Y

Histidine, His, H

Cysteine, Cys, C

Asparagine, Asn, N

Glutamine, Gln, Q

Tryptophan, Trp, W

Charged Amino Acids:

Aspartic Acid, Asp, D (negative charge)

Glutamic Acid, Glu, E (negative charge)

Lysine, Lys, K (positive charge)

Arginine, Arg, R (postive charge)

Special Symbols:

    Either Aspartic Acid or Asparagine, Asx, B

    Either Glutamic Acid or Glutamine, Gln, Z

    Unknown, X, X

 

Boise State University College of Engineering

Boise State University Department of Electrical and Computer Engineering

This page created by Dr. Scott F. Smith

This page was last updated on 06 March 2004.