Особливості планування і реалізації проектів ресторанного бізнесу

Ресторанний бізнес є однією із найбільш значущих складових індустрії гостинності. Водночас, ресторанний бізнес, з одного боку, є одним із засобів високоліквідного використання капіталу, а з іншого − середовищем із високим ступенем конкурентності. У всьому світі він є одним із найбільш розповсюджених видів малого бізнесу, тому заклади та підприємства ведуть між собою постійну боротьбу за сегментацію ринку, за пошук нових та за утримання постійних споживачів їхньої продукції та послуг. Всі заклади та підприємства повинні мати високий рівень конкурентоспроможності та мати свою унікальність

Hydrogen bonds formed between two strands.

<p>The black lines represent hydrogen bonds; residues in green are in the <i>strand</i> state. Hydrogen bonds are allowed to form when neighbouring residues are in a <i>strand</i> state and the side chains are oriented in the same parallel direction.</p

Analysis of the evolution of the structure of the oligomers over 11 independent simulations.

<p>(A) Development of the fraction of polypeptide chains in a oligomer (black), fraction of polypeptide chains in a oligomer that form a <i>β</i>-sheet conformation (blue), fraction of hydrogen bonds in a oligomer in a <i>α</i>-helical conformation (orange), and in a <i>β</i>-sheet conformation (red), or otherwise (green). (B) Development of the distribution function of the average number of <i>β</i>-sheets 〈<i>N_n</i>〉 of size <i>n</i> at <i>t</i> = 1000 (black), <i>t</i> = 5000 (red), <i>t</i> = 30 000 (blue). (C) Distribution function 〈<i>N_l</i>〉 of the number of protofilaments composed of <i>l</i> layers at <i>t</i> = 1000 (black), <i>t</i> = 15 000 (red), <i>t</i> = 30 000 (blue).</p

List of parameter values for the model.

<p>List of parameter values for the model.</p

Histogram of the number <i>N_n</i> of <i>β</i>-sheets consisting of <i>n</i> peptides at four successive stages of the growth and reordering process of the oligomeric assembly shown in Figure 1: (A) <i>t</i> = 10 000, (B) <i>t</i> = 15 000, (C) <i>t</i> = 20 000, (d) <i>t</i> = 30 000).

<p>This plot shows how <i>β</i>-sheet assemblies are progressively formed by the growth and alignment of individual <i>β</i>-sheets. At <i>t</i> = 10 000 (A) there are six <i>β</i>-sheets of sizes ranging from 3 to 16, whereas at <i>t</i> = 30 000 (D), there are nine <i>β</i>-sheets of sizes ranging from 8 to 42. If <i>β</i>-sheets are aligned so that the angle between them is smaller than 20 degrees, they are considered to form a protofilament-like structure, and the corresponding bars in the histogram are shown with the same color, as for instance in the case of the red assembly (<a href="http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.1000222#pcbi-1000222-g001" target="_blank">Figure 1c</a>, right), formed by four <i>β</i>-sheets of size 8, 19, 38, and 42.</p

Folding chacteristics and specificity.

<p>Folding characteristics are shown for a protein sequence that is designed to fold in a specific structure, and a random protein sequence; both sequences contain 35 residues and have a similar amino acid composition (see Methods). (a) Heat capacity versus temperature. A peak in the heat capacity curve can be observed at the folding transition. (b) Number of native contacts versus temperature. (c) Number of hydrogen bonds versus temperature. From the statistics it is clear that the sequence designed to fold shows a much sharper transitions than a random sequence of the same length. Moreover, the number of hydrogen bonds formed is strongly dependent on the sequence. Please refer to the Methods and Supplement for the sequences and structures used.</p

Illustration of the self-assembly process of peptides into amyloid-like assemblies.

<p>All simulations were carried out at a concentration <i>c</i> = 12.5 mM and reduced temperature <i>T</i>* = 0.66. The progress variable <i>t</i> corresponds to the number of Monte Carlo moves performed in the simulation, and one unit of <i>t</i> is a series of 10⁵ Monte Carlo moves. Initially, at <i>t</i> = 1000 (A), all peptides are in a solvated state. As the simulation progresses, at <i>t</i> = 5000 (B), a hydrophobic collapse causes the formation of a disordered oligomer, which subsequently undergoes a structural reorganization into an amyloid-like assembly, at <i>t</i> = 30 000 (C), driven by the formation of ordered arrays of hydrogen bonds. Peptides that do not form intermolecular hydrogen bonds are shown in blue, while peptides that form intermolecular hydrogen bonds are assigned a random color, which is the same for peptides that belong to same <i>β</i>-sheet.</p

Stability of small fibrillar structures containing 10 peptides.

<p>(a) The ensemble average of external (intermolecular) contacts versus temperature for different peptide sequences. External contacts are contacts between different peptides. (b) The ensemble average of hydrogen bonds versus temperature for different peptide sequences. These simulations started from small fibrillar configuration containing 10 peptides with 7 residues and different sequence compositions (see legend). In the temperature regime relevant for folding (), only fibrils that could form a strong hydrophobic core (TFTFTFT) are stable, in this case the hydrophobic residues would point inwards, as shown in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0085185#pone-0085185-g003" target="_blank">Figure 3</a>.</p

Facing side chains that interact.

<p>The yellow residues interact due to their orientation: they are directed towards each other.</p

Parallel side chains that interact.

<p>The yellow residues interact, since they point in the same direction in a parallel fashion.</p