Correlation of hydrogen bond length and log<i>RBA</i> of <i>A</i>-ring and <i>B</i>/<i>C</i>-ring derivatives.

<p>The hydrogen bond length data were shown in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0074615#pone-0074615-t001" target="_blank"><b>Table 1</b></a>. The amino acids shown in the up right corner of each indicated that the hydrogen bonds were formed between 3-hydroxyl groups of the <i>A</i>-ring or <i>B</i>/<i>C</i>-ring derivatives and this specific amino acid in the binding pocket. The curve regression was performed according to the Inverse First Order equation y = y₀+ a/x.</p

Data_Sheet_1_Understanding creativity process through electroencephalography measurement on creativity-related cognitive factors.pdf

IntroductionNeurotechnology approaches, such as electroencephalography (EEG), can aid understanding of the cognitive processes behind creativity.MethodsTo identify and compare the EEG characteristics of creativity-related cognitive factors (remote association, common association, combination, recall, and retrieval), 30 participants were recruited to conduct an EEG induction study.ResultsFrom the event-related potential (ERP) results and spectral analysis, the study supports that creativity is related to the frontal lobe areas of the brain and common association is an unconscious process.DiscussionThe results help explain why some creativity-related cognitive factors are involved either more or less readily than others in the creative design process from workload aspects. This study identifies the part of the brain that is involved in the combination cognitive factor and detects the ERP results on cognitive factors. This study can be used by designers and researchers to further understand the cognitive processes of creativity.</p

The overlay of the ligand-binding domains (LBDs) of ERα and ERβ.

<p>The protein structures were shown in cartoon and colored green and magenta for ERα and ERβ, respectively. E₂ molecules were shown in stick and colored blue and red in ERα and ERβ LBD, respectively. α-Helixes and β-sheets in the ER LBDs are labeled according to references <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0074615#pone.0074615-Brzozowski1" target="_blank">[14]</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0074615#pone.0074615-Shiau1" target="_blank">[16]</a>. Helix 2 structures are missing in both <i>X</i>-ray structures.</p

The chemical structures of 17β-estradiol (E₂) and the 27 E₂ derivatives.

<p>The number of each carbon is labeled next to the atom in the E₂ structure. The names of the E₂ derivatives were shown in the upper left corner of each frame. The <i>RBA</i> values of the E₂ derivatives for ERα and ERβ (data from <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0074615#pone-0074615-t001" target="_blank"><b>Table 1</b></a> as % of <i>RBA</i> of E₂) were shown in the lower right corner of each frame. The numbers were rounded to the nearest integer due to space constraint.</p

Primers used in the site-directed mutagenesis study.

<p>The sequences that are changed for each of the mutant COX proteins developed in this study are marked with underlines.</p

Correlation between log<i>RBA</i> and binding energy calculated with equation (1) and data in Table 1.

<p>The correlation coefficient <i>r</i> value is shown in the figure.</p

Summary of current 3D structures of ERs in complex with various ligands (listed according to the chronological order of the publications).

<p>Summary of current 3D structures of ERs in complex with various ligands (listed according to the chronological order of the publications).</p

Overlay of docked and crystal structures of ERα LBD in complex with DES or E₂. A

<p>. Superimposed structures of docking result and the crystal structure of ERα LBD in complex with DES. The known crystal structure of ERα LBD in complex with DES (PDB code: 3ERD) was colored in yellow with DES colored in green. The docked DES was colored in orange and ERα LBD was colored in magenta. <b>B</b>. Superimposed structures of docking result and the crystal structure of ERα LBD in complex with E₂. The known crystal structure of ERα LBD in complex with E₂ (PDB code: 3ERE) was colored in yellow with E₂ colored in green. The docked E₂ was colored in orange and ERα LBD was colored in magenta. The green dashes indicated the hydrogen bonds formed. All the structures were shown in ball and stick. The atoms involved with hydrogen bond formation were colored according to the atom type, i.e. white for hydrogen, red for oxygen and blue for nitrogen. Hydrogen atoms in other amino acids were not shown.</p

Interactions of <i>A</i>-ring derivatives with ERα LBD determined by the molecular docking method.

<p>The green dashes indicate the hydrogen bonds formed. All the structures are shown in ball and stick. The amino acids were colored according to the atom type, i.e. green for carbon, red for oxygen, blue for nitrogen and white for hydrogen. Among the amino acids in the binding site, only E353, R394 and H524 were shown in this figure. E₂ was colored in red; 1-methyl-E₂ and 4-Methyl-E₂ were colored in magenta; 2-OH-E₂ and 4-OH-E₂ were colored in green; 2-Br-E₂ and 4-Br-E₂ were colored in blue; 2-MeO-E₂ and 4-MeO-E₂ were colored in yellow. <b>A</b>. Overlay of all the <i>A</i>-ring derivatives. <b>B</b>. Overlay of E₂, 1-methyl-E₂, 2-MeO-E₂, 2-OH-E₂ and 2-Br-E₂. <b>C</b>. Overlay of E₂, 4-methyl-E₂, 4-MeO-E₂, 4-OH-E₂ and 4-Br-E₂.</p

Interactions of <i>B</i>/<i>C</i>-ring (A) and <i>D</i>-ring derivatives (B) with ERα LBD determined by molecular docking.

<p>The green dashes indicate the hydrogen bonds formed. All the structures are shown in ball and stick. The amino acids were colored according to the atom type, i.e. green for carbon, red for oxygen, blue for nitrogen and white for hydrogen. Among the amino acids in the binding site, only E353, R394 and H524 are shown in this figure. E₂ was colored in white. The ligands were shown in the following different colors: in <b>panel A</b>, 6α-OH-E₂ (yellow), 6β-OH-E₂ (orange), 6-keto-E₂ (pink), 6-dehydro-E₂ (red), 7-dehydro-E₂ (magenta), 9(11)-dehydro-E₂ (light blue), 11α-OH-E₂ (purple) and 11 β-OH-E₂ (green); in <b>panel B</b>, E₁ (magenta) estriol (16α-OH-E₂) (yellow), 16β-OH-E₂ (orange), 16-keto-E₂ (pink), 17α-OH-E₂ (red), 15α-OH-E₃ (dark blue), 16α-OH-E₁ (light blue), 16-keto-E₁ (purple), 16α-OH-E₂-17α (brown), 16β-OH-E₂-17α (grey).</p