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Journal of Biomolecular Structure & Dynamics ISSN 0739-1102 Volume 28, Issue Number 4, February 2011 Adenine Press (2011) Comment Proteins will Fold Anyway!! http://www.jbsdonline.com Protein folding
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Proteins are composed of short chain structures called amino acid residues that are arranged in different ordered arrays to form highly ordered proteins, all of them belonging to the same species. The most abundant sequence in the protein molecules is the “SER”-proteins, so named because of their amino acid sequence which is found at the very end of the protein molecule. It serves mainly as the recognition signal and is present at the very tip of each protein membrane and hence is a crucial component for protein recognition. The peptide repeats at the end of the amino acids serve as attachment and binding signals to the peptide chains that the peptide chain is embedded in. The protein folding is controlled by the properties of the amino acid residues of the protein. Thus, the protein of E-coli-E-glucose has the long, single chain, hydrophobic amino acid residues with helical and aromatic side chains which form the folded protein, its structure is called polypeptide. It is the single chain version of the common Peptide acid of the peptidoglycan, hence the name polypeptide (4, 5, 6, 7, 8, 9, 10). The Peptide acid molecule is formed from the amino acid, ?-glutamic acid, at position 47 of its chain. In polypeptide-like structure are the monosaccharide, glucose and the poly(A), poly(G) and poly(D) glucose residues: 1, 2 and 3 respectively (11, 12, 13, 14, 15, 16, 17). The molecular structure of polypeptide and polyglutamine molecules is shown in. Figure shows the molecular structure of the polypeptide-like protein of E Coline glc-?-gluc-1 with the amino acids (A), the polypeptide chain (B), the polyglycosylation sites (C) and the sugar residues (DS) as well as the molecular structure of the polyglutamine-like protein of E Coline glc-?-gluc-3 with the amino acid chain (A) and the polysaccharide (B). In the first example a hydrophobic amino acid in the polypeptide chain forms a porphyrin ring.

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