学术图库

图库 1

Water molecules and hydrophobic layers of amino acid residues in the high resolution crystal structures of adrenergic (left) and opioid receptors (right).

图库 2

Three distinct rotamer conformations, namely YI,YII and YIII, of a highly conserved Tyr (Y7.53) residue in the NPxxY motif correlate with the formation of the internal water pathway and the functional state of GPCRs.

图库 3

A schematic view of three different rotamer conformations of the highly conserved Y7.53 residue. The activation of GPCR correlates with the forming of a continuous internal water pathway.

图库 4

The principal analysis (PCA) and root-mean square fluctuation incate the flexible region of an enzyme.

图库 5

Two dominant binding modes of RPA1163 substrates and their relative ligand binding energies. The substrates are shown in green ball-and-sticks. The binding energy calculations show that the favorable binding modes having a lower binding energy which determines the stereoselectivity of the substrate.

图库 6

MetaMD simulations sampled the substrate entrance pathway for catalysis.

图库 7

A gating mechanism of the serotonin 5-HT3 ligand-gated ion channel.

图库 8

In agonist-bound GPCRs, several trans-membrane helixes underwent striking shifts including: TM3, ~2Å; TM5, ~4Å; TM6, ~7Å

图库 9

The protein ligand-interaction fingerprint shows different contacting profiles between the agonist-bound GPCRs and the antagonist bound ones

图库 10

A continuous water channel is observed in the agonist bound GPCRs upon the activation, whereas two hydrophobic layers are observed blocking the water flux.

图库 11

The WebGL and HTML5 technology facilitate online macromolecular visualization and modern drug discovery.

图库 12

Depecting macromolecules with PyMol and Inkscape in an artistic way.