<p>The NMR structure of hIAPP<sub>1–37</sub> (+3) (PDB ID: 2L86, model 1) is in yellow <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0047150#pone.0047150-Nanga1" target="_blank">[12]</a>. The side chains of the NMR structure are shown using the stick model. The representative structure of the wild type hIAPP<sub>1–25</sub> is in cyan. The representative structures of S20G mutant are in magenta with the interhelical angle ≅40° and green with the interhelical angle ≅90° (L-shaped motif), respectively.</p
One− and two−dimensional nuclear magnetic resonance spectroscopy (1D and 2D NMR) and site−directed m...
One− and two−dimensional nuclear magnetic resonance spectroscopy (1D and 2D NMR) and site−directed m...
<p>Each row of the figure represents one PCA analysis and contains, from left to right, a conformer ...
<p>A) Superposition of wild type (orange) and H234A (magenta) dimers using only A chain for structur...
<p>Protein backbone is rendered in ribbons, whereas Phe103, Ser181 and Thr274[Ala/Ile] side chains a...
<p>Colors for α chain, β chain, peptide, MHC, and mutant side chains from the crystal structure are ...
<p>(<b>A</b>) Superposed conformations were selected by RMSDs clustering. Ribbon diagrams display th...
<p>(A) Ensemble of the 20 lowest-energy CYANA conformers, superimposed on the backbone atoms of the ...
<p><b>A</b> Superimposition of the six KpDsbA molecules (blue) in the asymmetric unit shows the limi...
<p>Alignment of the average KIX structure from the simulations of Glu626Ala mutant of KIX∶MLL comple...
<p>(A) Backbone superposition of the 20 lowest energy conformers of ONCFLG. The disordered linker se...
<p>Based on the protein sequence of hic22, the secondary structure prediction is performed by Phyre<...
<p>(A) Ensemble of the 50 lowest energy structures (out of 100 calculated) of wt p15HPpep with the C...
<p>(A) Ribbon diagram of the Y16A/F28A HNP1 dimer with hydrophilic (left panel) and hydrophobic (rig...
One− and two−dimensional nuclear magnetic resonance spectroscopy (1D and 2D NMR) and site−directed m...
One− and two−dimensional nuclear magnetic resonance spectroscopy (1D and 2D NMR) and site−directed m...
One− and two−dimensional nuclear magnetic resonance spectroscopy (1D and 2D NMR) and site−directed m...
<p>Each row of the figure represents one PCA analysis and contains, from left to right, a conformer ...
<p>A) Superposition of wild type (orange) and H234A (magenta) dimers using only A chain for structur...
<p>Protein backbone is rendered in ribbons, whereas Phe103, Ser181 and Thr274[Ala/Ile] side chains a...
<p>Colors for α chain, β chain, peptide, MHC, and mutant side chains from the crystal structure are ...
<p>(<b>A</b>) Superposed conformations were selected by RMSDs clustering. Ribbon diagrams display th...
<p>(A) Ensemble of the 20 lowest-energy CYANA conformers, superimposed on the backbone atoms of the ...
<p><b>A</b> Superimposition of the six KpDsbA molecules (blue) in the asymmetric unit shows the limi...
<p>Alignment of the average KIX structure from the simulations of Glu626Ala mutant of KIX∶MLL comple...
<p>(A) Backbone superposition of the 20 lowest energy conformers of ONCFLG. The disordered linker se...
<p>Based on the protein sequence of hic22, the secondary structure prediction is performed by Phyre<...
<p>(A) Ensemble of the 50 lowest energy structures (out of 100 calculated) of wt p15HPpep with the C...
<p>(A) Ribbon diagram of the Y16A/F28A HNP1 dimer with hydrophilic (left panel) and hydrophobic (rig...
One− and two−dimensional nuclear magnetic resonance spectroscopy (1D and 2D NMR) and site−directed m...
One− and two−dimensional nuclear magnetic resonance spectroscopy (1D and 2D NMR) and site−directed m...
One− and two−dimensional nuclear magnetic resonance spectroscopy (1D and 2D NMR) and site−directed m...
<p>Each row of the figure represents one PCA analysis and contains, from left to right, a conformer ...