Protein layer structure

The elasticity of the protein layer structure is supposed to act against the tendency of an emulsion or foam to collapse because it allows the stretching of the interface. This behaviour is most commonly observed for globular proteins, which adsorb, partially unfold, and then develop attractive protein-protein interactions (Dickinson, 1999a Wilde, 2000 Wilde et al., 2004). The strength of such an adsorbed layer, reflected in the value of the elastic modulus, and the stress at which the structure breaks down, can be successfully correlated with stability of protein-based emulsions and (more especially) protein-based foams (Hailing, 1981 Mitchell, 1986 Izmailova et al., 1999 Dickinson, 1999a). 

Efimov, A. V. Packing of a-helices in globular proteins. Layer-structure of globin hydrophobic cores. J. Molec. Biol. 134, 23-40 (1979). 

In addition to classification based on layer structure, proteins can be grouped according to the type and arrangement of secondary structure. There are four such broad groups antiparallel a-helix, parallel or mixed /3-sheet, antiparallel /3-sheet, and the small metal- and disulfide-rich proteins. 

Conti et al. (1996) solved the crystal structure of the P. pyralis luciferase at 2.0 A resolution. The protein is folded into two compact domains, a large N-terminal portion and a small C-terminal portion. The former portion consists of a /1-barrel and two /1-sheets. The sheets are flanked by a-helices to form an aflafia five-layered structure. The C-terminal portion of the molecule forms a distinct domain, which is separated from the N-terminal domain by a wide cleft. It is suggested that the two domains will close up in the course of the luminescence reaction. 

The Langmuir-Blodgett (LB) technique was successfully applied for the deposition of thin protein layers (Langmuir and Schaefer 1938, Tiede 1985, Lvov et al. 1991). LB organization of protein molecules in film not only preserved the structure and functionality of the molecules, but also resulted in the appearance of new, useful properties, such as enhanced thermal stability (Nicolini et al. 1993 Erokhin et al. 1995). 

Figure 15.14 Study of the sample from the Dogon statuette 71.1935.105.169. (a) Optical microphotograph (b) SEM micrograph showing the layer structure ToF SIMS images of (c) proteins, (d) polysaccharides and (e) stearic acid (f) superposition of the distribution of poly saccharides and stearic acid (see colour Plate 9)...

The 3D structure of a native protein (in aqueous solution) is only marginally thermodynamically stable and it is sensitive to changes in its environment. It is, therefore, not surprising that adsorption is often accompanied by rearrangements in the protein s 3D structure. It is commonly observed experimentally that the thickness of an adsorbed protein layer is comparable to the dimensions of the protein molecule in solution. It indicates that the adsorbed protein molecules remain compactly structured. 

Information concerning myelin structure is also available from electron microscope studies, which visualize myelin as a series of alternating dark and less dark lines (protein layers) separated by unstained zones (the lipid hydrocarbon chains) (Figs 4-4 to 4-7). There is asymmetry in the staining of the protein layers. The less dark, or intraperiod, line represents the closely apposed outer protein... 

Most of the metal-rich proteins form approximately cylindrical two-layer structures with either an up and down (rubredoxin, cytochrome c) or a Greek key (ferredoxin) topology, but in which the elements forming the cylinder are a mixture of helices, /3 strands, and more or less extended portions of the backbone. Cytochrome c3 is perhaps the ultimate example of an S-M protein, with four hemes in just over a hundred residues, and essentially no secondary structure at all except for one helix. 

The nucleus is separated from the cytoplasm by the nuclear envelope, which consists of the outer and inner nuclear membranes. Each of the two nuclear membranes has two layers, and the membranes are separated from each other by the perinuclear space. The outer nuclear membrane is continuous with the rough endoplasmic reticulum and is covered with ribosomes. The inner side of the membrane is covered with a protein layer (the nuclear lamina), in which the nuclear structures are anchored. 

Nacreous structure layer a layer consisting of stacked platy aragonite crystals in brick-like layers and an interstitial protein layer. 

Dickinson, E. (1999b). Adsorbed protein layers at fluid interfaces interactions, structure and surface rheology. Colloids and Surfaces B Biointerfaces, 15, 161-176. 

Based on experimental evidence from AFM, the physical mechanism of orogenic5 displacement was proposed (Mackie et al., 1999b, 2000, 2003). A crucial aspect of the mechanism is that the surfactant domains exert a lateral surface pressure which compresses the protein layer. The AFM data obtained by Mackie and co-workers (1999b) provided direct visual evidence, for the first time, of a gel-like protein network at the air-water interface, as well as a structural explanation of protein displacement by small-molecule surfactant. In essence, the process of orogenic5 displacement is assumed to involve three stages ... 

These detailed AFM studies of the structure of surfactant + protein layers have helped to explain the followings observations ... 

The so-called diphil sorbents fit into the class of protein-coated supports. In these phases, silica-modified particles are saturated with albumin, and the adsorbed and denatured protein layer is stabilized with glutaric dialdehyde (134). Due to their structure, these sorbents exhibit both hydrophilic and organophil (diphil) properties tliat give them their name. 

Above Concentric monomolecular layers on Rothamsted necrosis protein. Magnification 50,000. (Wyckoff, 1948.) Below spiral monomolecular layer structure on crystal of n-hexatriacontane, C8ftHu. Magnification 20,000. (Dawson and Vand, 1951)... 

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