In this, simplest, model, all turns of the helix closed on itself, although Figure 1 shows that this is not quite so. Each turn of the helix is open for the nearest neighbor. It was previously shown [6] that taking into account open individual cells leads only to quantitative changes. The qualitative picture remains unchanged. Figure 2 Simplest model of alpha-helix as a one-dimensional molecular crystal with three molecules per unit cell. Arrows are showing a separate

peptide group. They symbolize the dipole moments. Within the framework of the Ralimetinib cell line considered model, every three peptide groups that belong to one turn of the helix grouped into one complex unit cell. We will number these unit cells by indices n, m, etc. The number of such cells is three times less than the number of peptide groups, i.e., N 0/3. Peptide groups within a single cell will be enumerated by indices α, β, etc. that may ATM Kinase Inhibitor clinical trial take this website values 0, 1, 2. The general functional for the alpha-helix in this model has the form [7] w(R nα  − R mβ ) in this functional is the basic energy of interaction between peptide groups nα and mβ. It is independent on the presence of excitation and exists always. D(R nα  − R mβ )|A αn |2 is an additional energy to the w(R nα  − R mβ ) energy of interaction related only to excitation but considerably smaller. Factor A αn is the wave function that describes the excited

state of the examined alpha-helical region of the protein Verteporfin in vitro molecule. It determines the spatial-temporal distribution of excitation in this region. The energy D(R nα  − R mβ )|A αn |2 leads to the breaking of the equilibrium of the alpha-helix and stimulates its conformational response to excitement. Energy is also an additional energy of interaction. However, it is much less than D(R nα  − R mβ )|A αn |2 but important because it provides the propagation and transfer of excitation along the alpha-helix. As shown in Figure 2, the nearest neighbors for some peptide group nα will only be the peptide groups m = n ± 1, β = α and m = n, β = α ± 1. Taking into account

that in the considered model all energy terms depend on the distances between amino acid residues only, the following formulae in the nearest neighbor approximation may be obtained: R nα  ≡ |R n + 1,α  − R n,α |, ρ nα  ≡ |R n,α + 1 − R n,α |. Let us take into account that the response of the lattice (Figure 2) on excitation inside of the unit cell is small enough. Thus, it may be neglected in comparison with a similar response between unit cells. In this sense, the equality ρ nα  = ρ 0 is always supposed fulfilled. Factor R nα is the only value that takes into account the response of the alpha-helix on excitation. Thus, we will denote its equilibrium value as R 0. Values ρ 0 and R 0 are shown in Figure 2. Taking into account the normalization condition (1) the last functional takes the form (2) Here, w ⊥ ≡ w(ρ 0), D ⊥ ≡ D(ρ 0), M ⊥ = M(ρ 0), and M || = M(R 0).