선택한 단어 수는 입니다.
최소 단어 이상 선택하여야 합니다.
최소 단어 이상 선택하여야 합니다.
선택한 단어 수는 30입니다.
최대 10 단어까지만 선택 가능합니다.
최대 10 단어까지만 선택 가능합니다.
가설 설정
- 1 Å). The distribution of Cα root-mean-square fluctuation (RMSF) is shown in Figure 2. The helix 1 and helix 2 regions exhibit less fluctuations compared to the loop region. The averaged secondary structural data are shown in Figure 3.
- The helix 1 and helix 2 regions exhibit less fluctuations compared to the loop region. The averaged secondary structural data are shown in Figure 3. The averaged helicity (61%) of the entire structure during the simulations is considerably high. In the more details, based on the residuespecific secondary structure calculations, high helical character on the entire helices sequence (residues 2-16 and 24-38) is indicated, whereas the thioether bond and loop region are indicated less than that of the helix region.
- In the more details, based on the residuespecific secondary structure calculations, high helical character on the entire helices sequence (residues 2-16 and 24-38) is indicated, whereas the thioether bond and loop region are indicated less than that of the helix region. The high helical character of the cHLH peptide mainly arises from the salt-bridge formation on the helix 1 and hydrophobic interactions on the helix 2. Firstly, salt-bridge formation on the helix 1 is important to maintain the helical character of the cHLH peptide. The six grafted arginine residues (R3, R6, R7, R10, R13, and R14) interact with four Especially, for F30 and W34, they interact each other to make T-shaped π-π stacking interactions.
- The epitope residues are inserted into the cleft. d) It is X-Ray structure of the p53 complex with the HDM2. (Epitope residues are magenta-colored stick.
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