Journal: Prion

Article Title: Quantum dots and prion proteins

doi: 10.4161/pri.26524

Figure Lengend Snippet: Figure 1. Three-dimensional (3D) structure of human PrP. The structure of the α-helical form of rPrP(90–231) resembles that of PrPC. rPrP(90–231) is viewed from the interface where PrPSc is thought to bind to PrPC. The color scheme is as follows: α-helices A (residues 144–157), B (172–193), and C (200–227) in pink; disulphide between Cys-179 and Cys-214 in yellow; conserved hydrophobic region composed of residues 113–126 in red; loops in gray; residues 129–134 in green encompassing strand S1 and residues 159–165 in blue encompassing strand S2; the arrows span residues 129–131 and 161–163, as these show a closer resemblance to β-sheet (155).1 The data source was the internet proteomic database Expasy (www.expasy.org). For data processing software Matlab version 7.9.0 (The MathWorks, Inc.) was used.

Article Snippet: For data processing software Matlab version 7.9.0 (The MathWorks, Inc.) was used.

Techniques: Software