by Auguste Rodin.
(A great artists beautiful illustration what the
"affinity" is about....)
| Affinity Proteins (AP) are short oligo-peptides which have strong and specific affinity to their
query proteins (QP). Additionally all AffiSeq® peptides have a common biochemical feature:
codons which are coding co-locating (interacting) amino acids in AP and QP are complementary
to each other, in reverse orientation, in their 1st and 3rd bases, while the 2nd (central) bases may
but not necessarily complementary to each other (like 5’-ATG-3’/3’-TNC-5’). This rule of "partially
complementary coding of co-locating amino acids" is described in the concept of Proteomic
Code  which is part of the Nierenberg’s Genetic Code [2, 3]. The concept emphasizes the
role of exact coding sequences (including wobble bases) in coding of exact 3D protein structures
in addition to the amino acid sequences (see the concept of Nucleic Acid Chaperons, ).
AffiSeq® is the registered Trade Mark of all Affinity Proteins which are designed by the rules
and concept of Proteomic Code.
 Biro JC: The Proteomic Code: a molecular recognition code for proteins. Review Article, J. Theor Biol Med Modeling, 2007. 4:45,
 Nirenberg MW, Matthaei JH: The dependence of cell-free protein synthesis in E. coli upon naturally occurring or synthetic
polyribonucleotides. PNAS USA 1961, 47:1588–1602.
 Biro JC: The Invention of Proteomic Code and mRNA Assisted Protein Folding. 2008. Cite as: arXiv:0808.0043v1 [q-bio.BM]
 Biro JC: Nucleic Acid Chaperons: A theory of an RNA-assisted Protein Folding. Theor Biol Med Model. 1;2:35, 2005