The crystallographic tetramer of aromatase and validation of the C_α normal mode analysis against crystallographic B factors.

<p>A, three aromatase monomers from one oligomer chain (ribbon diagram colored blue, green and orange) in contact through the H-I loops with another monomer (gray) from the neighboring chain. B, the computed B-factors of C_α of the central monomer (green line), simulating the closely packed aromatase in crystals, are compared well with those from X-ray data (black line). The substrate and heme group are represented by stick drawings. The former is colored in magenta while the latter is rendered in element colors: cyan, C; red, O; blue, N; brown, Fe. The coloring code and the atoms and bonds representations are the same in all figures unless otherwise noted.</p

Plot of observed score process and bootstrapped processes of time to withdrawal of study with respect to <i>Z</i>₁.

<p><b>The thickline is observed process and the dashed lines are bootstrapped processes</b>.</p

Intermolecular motions of the aromatase trimers from normal mode analysis and their complementarity with electrostatic interactions.

<p>A, two slowest normal modes in aromatase trimer. The dotted lines designate the rotational axes. B, electrostatic potentials mapped on the van der Waals surfaces of a trimer in a color scale red to blue representing a potential scale from −7<i>k</i>T/e to 7<i>k</i>T/e. The P and E sites, adjacent to the head-to-tail binding interfaces of the oligomers, correspond to the positively and negatively charged cavities, respectively. The arrow points roughly along the electrostatic potential gradient from negative to positive potentials. The orientation of oligomer is roughly the same in both panels. The inset shows the second dimer interface hidden from view.</p

Point estimates with standard errors of covariates in AIDS study for model without New3TC (Standard errors are shown in parenthesis).

<p>¹ efavirenz</p><p>² nelfinavir</p><p>³ logarithm of RNA at the start of the study</p><p>Point estimates with standard errors of covariates in AIDS study for model without New3TC (Standard errors are shown in parenthesis).</p

Transformation of a linear to a circular hexamer that has the correct membrane insertion topology.

<p>A, a linear hexamer (a chain of two units of trimers) related by the crystallographic 3₂ screw symmetry. B and C, the plan and cross-section of a circular hexamer inserted within a lipid bilayer.</p

Intramolecular modes of motion of a membrane-free monomer and a membrane-integrated monomer by normal mode analysis.

<p>A, the three moving parts of a membrane-free monomer in the mode 7 producing the hinge-bending motions with the hinge at the active site access channel. B, two moving parts in mode 8 contributing to a twisting motion with the access channel at the interface. C and D, two internal normal modes (modes 19 and 17) show the intramolecular bending and twisting motions for a membrane-integrated monomer. The residues of the access channel are represented by sticks and rendered in orange color. The residues include Arg192, Ile217, Gln218, Phe221, Asp222, Ala225, Pro308, Asp309, Thr310, Ser312, Val313, Val369, Ile474, Ser478, Leu479, His480, Pro481, Asn482, Glu483 and Thr484. The eigenvector arrows are in the same indication as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0032565#pone-0032565-g002" target="_blank">Fig. 2 (C)</a> while the large arrows depict the direction of collective motions.</p

Plot of observed score process and bootstrapped processes of time to first virologic failure using α^L with respect to <i>Z</i>₁.

<p><b>The thickline is observed process and the dashed lines are bootstrapped processes</b>.</p

Module structure of interphotoreceptor retinoid-binding protein (IRBP) may provide bases for its complex role in the visual cycle – -9

<p><b>Copyright information:</b></p><p>Taken from "Module structure of interphotoreceptor retinoid-binding protein (IRBP) may provide bases for its complex role in the visual cycle – "</p><p>http://www.biomedcentral.com/1471-2091/8/15</p><p>BMC Biochemistry 2007;8():15-15.</p><p>Published online 4 Aug 2007</p><p>PMCID:PMC2000878.</p><p></p>tation, 330 nm; emission, 480 nm). The concentration of the IRBP double module was: modules 1&2, 0.67 μM; modules 3&4, 0.57 μM. IRBP modules 1&2 showed = 2.45 ± 0.11 with = 0.049 ± 0.023 μM. IRBP modules 3&4 showed N = 1.43 ± 0.21 with = 0.19 ± 0.05 μM

Module structure of interphotoreceptor retinoid-binding protein (IRBP) may provide bases for its complex role in the visual cycle – -13

<p><b>Copyright information:</b></p><p>Taken from "Module structure of interphotoreceptor retinoid-binding protein (IRBP) may provide bases for its complex role in the visual cycle – "</p><p>http://www.biomedcentral.com/1471-2091/8/15</p><p>BMC Biochemistry 2007;8():15-15.</p><p>Published online 4 Aug 2007</p><p>PMCID:PMC2000878.</p><p></p> 1 through 4. The numbering on the axes correspond with the amino acid residues in Figure 2. The diagonal lines indicate regions of internal similarity, and hence the presence of the four modules. Distance tree showing the relationship between , human, bovine, goldfish and zebrafish IRBPs. The branch lengths are drawn to scale and the values at the nodes indicate the number of times a grouping occurred in a set of 100 bootstrap values. The long distance separating the teleosts from amphibians is due in part to the teleosts having only two modules

Module structure of interphotoreceptor retinoid-binding protein (IRBP) may provide bases for its complex role in the visual cycle – -5

<p><b>Copyright information:</b></p><p>Taken from "Module structure of interphotoreceptor retinoid-binding protein (IRBP) may provide bases for its complex role in the visual cycle – "</p><p>http://www.biomedcentral.com/1471-2091/8/15</p><p>BMC Biochemistry 2007;8():15-15.</p><p>Published online 4 Aug 2007</p><p>PMCID:PMC2000878.</p><p></p>ll-retinol in solution was 3.2 μM. The degradation of all-retinol was monitored by measuring its absorbance at 325 nm as a function of time. For each sample, absorbance measurements were made every 2 min for 72 minutes. Full-length IRBP (filled circles) is able to protect all-retinol from degradation as compared to a PBS control (unfilled circles)