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1. Data File S1: Ethical Statement for the Present Study. 2. Data File S2: Data of BIRD-Form. 3. Data File S3: Data of BIRD-WinForms. [^1]: Edited by: Geertje van den Biggelaar, University of California, Davis, United States [^2]: Reviewed by: Geertje van den Biggelaar, University of California, Davis, United States; Carolina Varoqui, Universidad Nacional de Asunción, Paraguay [^3]: This article was submitted to Performance Science, a section of the journal Frontiers in Psychology Various methods of modifying the N-terminal amino acid residues of proteins have been described. For example, it is known to genetically modify the N-terminal amino acid residue of a polypeptide by in vitro recombinant DNA methods using bacteriophage or plasmid expression systems. Methods of making N-terminal modifications of proteins, for example N-terminal modification by acetylation or pyroglutamylation, have also been described. See, for example, U.S. Pat. No. 5,661,018 and U.S. Pat. No. 5,260,203. The term “N-terminus” is used herein to mean that amino acid residue which, when a protein is expressed in a cell-free environment, initiates the translation of a polypeptide and which is, in the primary structure of the protein, the amino acid residue first in the amino acid sequence. Disulfide-containing proteins have also been previously described. The chemical crosslinking of disulfide bonds in proteins has been used to produce dimers or higher order oligomers from monomers. See, for example, Barichello, J. Biol. Chem. 256, 9274 (1981); Klein, Curr. Op. Cell. Biol. 1, 561 (1989); and Bertolino, Prog. Nuc. Acid Res. Mol. Biol. 42, 23 (1994). Protein assembly has also been accomplished by using recombinant DNA technology to produce protein polymers in cell-free protein expression systems. For example, a chemically cross-linked protein polymer has been produced from an aqueous solution of recombinantly produced glutamine synthetase by in vitro expression in

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