Aromatic polypeptides

Antibiotic A201A. Antibiotic A201A (23), produced by S. capreolus is an /V -dimethyladenine nucleoside stmcturaHy similar to puromycin (19). Compound (23) which contains an aromatic acid and monosaccharide residues (1,4), inhibits the incorporation of amino acids into proteins but has no effect on RNA or DNA synthesis. Compound (23) does not accept polypeptides as does (19), and does appear to block formation of the initiation complex of the SOS subunit. It may block formation of a puromycin-reactive ribosome. 

Even though these enzymes have no absolute specificity, many of them show a preference for a particular side chain before the scissile bond as seen from the amino end of the polypeptide chain. The preference of chymotrypsin to cleave after large aromatic side chains and of trypsin to cleave after Lys or Arg side chains is exploited when these enzymes are used to produce peptides suitable for amino acid sequence determination and fingerprinting. In each case, the preferred side chain is oriented so as to fit into a pocket of the enzyme called the specificity pocket. 

Figure 11.11 Schematic diagrams of the specificity pockets of chymotrypsin, trypsin and elastase, illustrating the preference for a side chain adjacent to the scisslle bond In polypeptide substrates. Chymotrypsin prefers aromatic side chains and trypsin prefers positively charged side chains that can interact with Asp 189 at the bottom of the specificity pocket. The pocket is blocked in elastase, which therefore prefers small uncharged side chains.

Chymotrypsin-like proteinases are serine proteinases that recognize pqDtide residues with aromatic side chains (phyenylalanyl or tyrosyl residues) and that effect hydrolysis of the polypeptide chain on the carboxy-terminal side of these residues. Examples of chymotrypsin-like proteinases are chymotrypsin and cathepsin-G. 

Polyamides are macromolecules with acidamide units —CONH—, where the chemical structure of the other parts of the monomers can be aliphatic and/or aromatic. Similar structures are found in nature, for example, polypeptides. Although in principle a large number of potential polyamide structures can be produced, only a few polyamides are produced in industrial scale. 

There are at least three types of PKS. Type I PKSs catalyze the biosynthesis of macrolides such as erythromycin and rapamycin. As modular enzymes, they contain separate catalytic modules for each reaction catalyzed sequentially in the polyketide biosynthetic pathway. Type II PKSs have only a few active sites on separate polypeptides, and the active sites are used iteratively, catalyzing the biosynthesis of bacterial aromatic polyketides. Type III are fungal PKSs they are hybrids of type I and type II PKSs [49,50]. 

No, K. T., J. A. Grant, M. S. Jhon, and H. A. Scheraga. 1990. Determination of Net Atomic Charges Using a Modified Partial Equalization of Orbital Electronegativity Method 2. Application to Ionic and Aromatic Molecules as Models for Polypeptides. J. Phys. Chem. 94, 4740-4746. 

The influence of adsorption on the structure of a -chymotrypsin is shown in Fig. 10, where the circular dichroism (CD) spectrum of the protein in solution is compared with that of the protein adsorbed on Teflon and silica. Because of absorbance in the far UV by the aromatic styrene, it is impossible to obtain reliable CD spectra of proteins adsorbed on PS and PS- (EO)8. The CD spectrum of a protein reflects its composition of secondary structural elements (a -helices, / -sheets). The spectrum of dissolved a-chymotrypsin is indicative of a low content of or-helices and a high content of //-sheets. After adsorption at the silica surface, the CD spectrum is shifted, but the shift is much more pronounced when the protein was adsorbed at the Teflon surface. The shifts are in opposite directions for the hydrophobic and hydrophilic surfaces, respectively. The spectrum of the protein on the hydrophilic surface of silica indicates a decrease in ordered secondary structure, i.e., the polypeptide chain in the protein has an increased random structure and, hence, a larger conformational entropy. Adsorption on the hydrophobic Teflon surface induces the formation of ordered structural elements, notably an increase in the content of O -helices (cfi, the discussion in Sect. 3.1.4). 

The percent conversion of the monomer to the polypeptide can be estimated by the quantity 100 (Aq - At) / Aq, where Aq and At are the integrated intensities of the ester band at the start and time t, respectively. At 40 °C, it tended to saturate at about 30 % for the Y-type films of L-NaphAla-C-i s, and L-PyrAla-G 8, although the conversion for the LB film of long-chain ester of alanine (L-Ala- Ci s) reached to 90 % [52]. This difference is considered to be due to a larger steric hindrance of the aromatic rings. 

Polymers and resins Water purification, including removal of phenol, chlorophenols, ketones, alcohols, aromatics, aniline, indene, polynuclear aromatics, nitro- and chlor-aromatics, PCB, pesticides, antibiotics, detergents, emulsifiers, wetting agents, kraftmill effluents, dyestuffs recovery and purification of steroids, amino acids and polypeptides separation of fatty adds from water and toluene separation of aromatics from ahphatics separation of hydroquinone from monomers recovery of proteins and enzymes removal of colours from symps ... 

J. B. A. Ross, W. R. Laws, J. C. Sutherland, A. Buku, P. G. Katsoyannis, I. L. Schwartz, and H. R. Wyssbrod, Linked-function analysis of fluorescence decay kinetics Resolution of side-chain rotamer populations of a single aromatic amino acid in small polypeptides, Photochem. Photobiol. 44, 365-370 (1986). 

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