Polypeptides characteristics

Table 22.1. C chemical shifts of polypeptides characteristic of a-helix, j8-sheet and oi-helix forms...

The biosynthesis of a variety of biologically active peptides proceeds nucleic acid-free on protein templates (IK Peptide synthetases generally activate an acceptor amino acid by formation of amino-acyl adenylates or phosphates, which will be stabilized in an enzyne-aminoacylation step, similar as in tRNA-aminoacylation. Reaction with a donor peptide, which may be covalently bound, leads to a specific chain elongation. While small peptides like glutathione are formed by "one-step"-synthetases, more complex structures like gramicidin S are produced by multienzvme systems, which may contain multifunctional polypeptides. Characteristic features of such systems are 1.)activation as aminoacyl adenylates, 2.) aminoacylation of enzyme thiol-groups, 3.) covalently bound peptide intermediates and 4.) a specific intrinsic transport mechanism similar to the biosynthesis of fatty acids. 

In tire simple version of tire lattice representation of proteins tire polypeptide chain is modelled as a sequence of connected beads. The beads are confined to tire sites of a suitable lattice. Most of tire studies have used tire cubic lattice. To satisfy tire excluded volume condition only one bead is allowed to occupy a lattice site. If all tire beads are identical we have a homopolymer model the characteristics of which on lattices have been extensively studied. 

Transfer RNA (tRNA) Transfer RNAs are relatively small nucleic acids containing only about 70 nucleotides They get their name because they transfer ammo acids to the ribosome for incorporation into a polypeptide Although 20 ammo acids need to be transferred there are 50-60 tRNAs some of which transfer the same ammo acids Figure 28 11 shows the structure of phenylalanine tRNA (tRNA ) Like all tRNAs it IS composed of a single strand with a characteristic shape that results from the presence of paired bases m some regions and their absence m others... 

The unique characteristic of each protein is the distinctive sequence of amino acid residues in its polypeptide chain(s). Indeed, it is the amino acid sequence of proteins that is encoded by the nucleotide sequence of DNA. This amino acid sequence, then, is a form of genetic information. By convention, the amino acid sequence is read from the N-terminal end of the polypeptide chain through to the C-terminal end. As an example, every molecule of ribonucle-... 

Many proteins consist of two or more interacting polypeptide chains of characteristic tertiary structure, each of which is commonly referred to as a subunit of the protein. Subunit organization constitutes another level in the hierarchy of protein structure, defined as the protein s quaternary (4°) structure (Figure 5.10). Questions of quaternary structure address the various kinds of subunits within a protein molecule, the number of each, and the ways in which they interact with one another. 

Ribosomal RNAs characteristically contain a number of specially modified nucleotides, including pseudouridine residues, ribothymidylic acid, and methylated bases (Figure 11.26). The central role of ribosomes in the biosynthesis of proteins is treated in detail in Chapter 33. Here we briefly note the significant point that genetic information in the nucleotide sequence of an mRNA is translated into the amino acid sequence of a polypeptide chain by ribosomes. 

Transfer RNA (tRNA) serves as a carrier of amino acid residues for protein synthesis. Transfer RNA molecules also fold into a characteristic secondary structure (marginal figure). The amino acid is attached as an aminoacyl ester to the 3 -terminus of the tRNA. Aminoacyl-tRNAs are the substrates for protein biosynthesis. The tRNAs are the smallest RNAs (size range—23 to 30 kD) and contain 73 to 94 residues, a substantial number of which are methylated or otherwise unusually modified. Transfer RNA derives its name from its role as the carrier of amino acids during the process of protein synthesis (see Chapters 32 and 33). Each of the 20 amino acids of proteins has at least one unique tRNA species dedicated to chauffeuring its delivery to ribosomes for insertion into growing polypeptide chains, and some amino acids are served by several tRNAs. For example, five different tRNAs act in the transfer of leucine into... 

The secondary structure of a protein is the shape adopted by the polypeptide chain—in particular, how it coils or forms sheets. The order of the amino acids in the chain controls the secondary structure, because their intermolecular forces hold the chains together. The most common secondary structure in animal proteins is the a helix, a helical conformation of a polypeptide chain held in place by hydrogen bonds between residues (Fig. 19.19). One alternative secondary structure is the P sheet, which is characteristic of the protein that we know as silk. In silk, protein... 

In the presence of air, the roots, coleoptile, mesocotyl, endosperm, scutellum, and anther wall of maize synthesise a tissue-specific spectrum of polypeptides. The scutellum and endosperm of the immature kernel synthesise many or all of the ANPs constitutively, along with many other proteins under aerobic conditions. Under anaerobic conditions all of the above organs selectively synthesise only the ANPs. Moreover, except for a few characteristic qualitative and quantitative differences, the patterns of anaerobic protein synthesis in these diverse organs are remarkably similar (Okimoto et al., 1980). On the other hand, maize leaves, which have emerged from the coleoptile, do not incorporate labelled amino acids under anaerobic conditions and do not survive even a brief exposure to anaerobiosis (Okimoto et al., 1980). 

This polypeptide is structurally identical to ABA-type triblock copolymer with a central hydrophdic elastomeric end-block capped with two hydrophobic plastic end-blocks and exhibits amphiphilic characteristics. The end-blocks of the polymer were chosen in such a way that their LCST would reside at or near room temperature. Thus the polymer exhibits phase separation, which is analogue to conventional TPEs, and offers TPE gels under physiological relevant conditions [104]. Glutamic acid residue is placed periodically in the elastomeric mid-block to increase its affinity towards the aqueous... 

The first elastomeric protein is elastin, this structural protein is one of the main components of the extracellular matrix, which provides stmctural integrity to the tissues and organs of the body. This highly crosslinked and therefore insoluble protein is the essential element of elastic fibers, which induce elasticity to tissue of lung, skin, and arteries. In these fibers, elastin forms the internal core, which is interspersed with microfibrils [1,2]. Not only this biopolymer but also its precursor material, tropoelastin, have inspired materials scientists for many years. The most interesting characteristic of the precursor is its ability to self-assemble under physiological conditions, thereby demonstrating a lower critical solution temperature (LCST) behavior. This specific property has led to the development of a new class of synthetic polypeptides that mimic elastin in its composition and are therefore also known as elastin-like polypeptides (ELPs). 

The ionized forms of polypeptides exhibit many characteristics in common therefore, we have studied them under various conditions. The most interesting observation is the transition of a polyelectrolyte brush found by changing the polyelectrolyte chain density. The brush layers have been prepared by means of the LB film deposition of an amphiphile, 2C18PLGA(48), at pH 10. Mixed monolayers of 2C18PLGA(48) and dioctadecylphos-phoric acid, DOP, were used in order to vary the 2C18PLGA(48) content in the monolayer. 

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