Helicate triple

The T4 short tail fiber triple /l-helix is connected to a more globular head domain via residues 333-341, which form a very short a-helical triple coiled-coil. Residues 342-396, together with the C-terminal /1-strand composed of amino acids 518-527 (the collar ), are the only part of the structure in which the monomer has a recognizable fold. It may therefore be the first part of the protein to fold, followed by a zipping-up of the N-terminal domain and the top domain. The small, globular, domain contains six /1-strands and one a-helix and has some structural homology to gpl 1, also of bacteriophage T4. Three of the /1-strands and the a-helix formed by residues... 

Macroconformations consisting of two or three helices intertwined with each other are also sometimes called super helices or super secondary structures. An example is deoxyribonucleic acid, which forms a double helix from two complementary chains, each in the form of a helix (see Section 29). With synthetic polymers, both it-poly(methyl methacrylate) and poly(/ -hydroxybenzoic acid) appear to form double helices. Triple helices are, for example, formed by the protein, collagen (see Section 30). 

FIGURE 19.12 (See color insert.) VPL motor at (a) neutral and (b) acidic pH. (a) Front view of the partially a-helical triple stranded coiled coil. VPL motor is in the closed conformation, (b) VPL Motor in the open conformation. The random coil regions (white) are converted into well-defined helices and an extension occurs at lower pH. 

Not all DNAs are double helices duplex DNA) Some types of viral DNA are single stranded and even a few DNA triple and quadruple helices are known... 

Fibrous proteins can serve as structural materials for the same reason that other polymers do they are long-chain molecules. By cross-linking, interleaving and intertwining the proper combination of individual long-chain molecules, bulk properties are obtained that can serve many different functions. Fibrous proteins are usually divided in three different groups dependent on the secondary structure of the individual molecules coiled-coil a helices present in keratin and myosin, the triple helix in collagen, and P sheets in amyloid fibers and silks. 

Fibrous proteins are long-chain polymers that are used as structural materials. Most contain specific repetitive amino acid sequences and fall into one of three groups coiled-coil a helices as in keratin and myosin triple helices as in collagen and p sheets as in silk and amyloid fibrils. 

FIGURE 6.18 Poly(Gly-Pro-Pro), a collagen-like right-handed triple helix composed of three left-handed helical chains. (Adaptedfrom Miller Scheraga, H. A., 1976, Calculation of the... 

Exopolysaccharides in solution have an ordered helical conformation, which may be single, double or triple for example, xanthan forms a double or triple helix (Figure 7.3c). These are stabilised by intermolecular hydrogen bonds. The helical conformation makes the exopolysaccharide semirigid and the molecules can move large volumes of solution. These volumes overlap even at low concentrations of exopolysaccharide, giving rise to relatively high viscosities. 

Curdlan possesses anti-tumour activity similar to that shown by fungal (1-D-glucans, a property which appears to be related to the ability to form triple helices. 

Collagen-like (ColQ) tailed forms or asymmetric multimers Characterized by triple helical structure of three collagenic subunits Q, each associated with... 

In the case of cooperative processes, the formation of a nucleus, already discussed from the kinetical point of view, plays a crucial role. The steady state described by Eq. (1) depicts the formation of a triple helix as the simplest model by the formation of a nucleus Hx through fast pre-equilibria and subsequent propagation steps, Hx in this case is a triple-helical intermediate with x tripeptide units (that means x hydrogen bonds) in the helical state. The final product H3n 2 possesses two hydrogen bonds less than tripeptide units because the three single chains are staggered at one amino add residue each. 

Since 1973, several authors have proved that there is a relationship between thermostability of collagen and the extent of hydroxylation of the proline residues31,34). Equilibrium measurements of the peptides al-CB 2 of rat tail and rat skin revealed a higher rm, for al-CB 2 (rat skin)157). The sequence of both peptides is identical except that in the peptide obtained from rat skin, the hydroxylation of the proline residues in position 3 has occurred to a higher extent than in the case of al-CB 2 (rat tail). Thus, a mere difference of 1.8 hydroxy residues per chain causes a ATm of 26 K. Obviously, there are different stabilizing interactions in the triple-helical state, that means al-CB 2 (rat skin) forms more exothermic bonds than al-CB 2 (rat tail) in the coil triple-helix transition. This leads to an additional gain of enthalpy which overcompensates the meanwhile occurring losses of entropy. 

It is known that native collagen contains tripeptide sequences which, because of being homopolypeptides, are not able to give rise to triple-helical tertiary structures (e.g. Gly-Pro-Leu, Gly-Pro-Ser). The reason for this and for the above-mentioned low thermostability of the synthetic homopolypeptides is presumably to be found in the fact that in the case of the model peptides with their monotonously repeated tripeptide sequences, special interactions between the side chains of the different amino acid residues as postulated by Ward and Mason are no more possible157). 

Fig. 21.—Structure of the 6-fold anhydrous curdlan III (19) helix, (a) Stereo view of a full turn of the parallel triple helix. The three strands are distinguished by thin bonds, open bonds, and filled bonds, respectively. In addition to intrachain hydrogen bonds, the triplex shows a triad of 2-OH - 0-2 interchain hydrogen bonds around the helix axis (vertical line) at intervals of 2.94 A. (b) A c-axis projection of the unit cell contents illustrates how the 6-0H - 0-4 hydrogen bonds between triple helices stabilize the crystalline lattice.

Figured. Diagrammatic representation of the red blood cell cytoskeletal-plasma membrane complex. Spectrin is made up of many homologous triple-helical segments joined by nonhelical regions (Speicher and Marchesi, 1984). Spectrin and actin require accessory proteins to form a membrane-associated network. (This diagram is constructed from data previously published for example, see Stryer, 1988 Davies and Lux, 1989 Bennett and Gilligan, 1993).

Speicher, D.W. Marchesi, V.T. (1984). Erythrocyte spectrin is comprised of many homologous triple helical segments. Nature 311, 177—180. 

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