Display Settings:

Items per page
We are sorry, but NCBI web applications do not support your browser and may not function properly. More information

Results: 7

1.
Figure 4

Figure 4. From: The core of Ure2p prion fibrils is formed by the N-terminal segment in a parallel cross-? structure: Evidence from solid state NMR.

2D 13C-13C NMR spectra of unseeded Ure2p fibrils before (a,b) and after (c,d) proteinase K treatment. Contour levels increase by successive factors of 1.5 (a,c) or 1.3 (b,d).

Dmitry S. Kryndushkin, et al. J Mol Biol. ;409(2):263-277.
2.
Figure 1

Figure 1. From: The core of Ure2p prion fibrils is formed by the N-terminal segment in a parallel cross-? structure: Evidence from solid state NMR.

TEM images of prion-seeded (a,b) and unseeded (c,d) Ure2p fibrils before (a,c) and after (b,d) proteinase K treatment. TEM grids are negatively stained with uranyl acetate. Scale bars are 200 nm.

Dmitry S. Kryndushkin, et al. J Mol Biol. ;409(2):263-277.
3.
Figure 3

Figure 3. From: The core of Ure2p prion fibrils is formed by the N-terminal segment in a parallel cross-? structure: Evidence from solid state NMR.

2D 15N-13C spectra of prion-seeded Ure2p fibrils before (a) and after (c) proteinase K treatment (same samples as in Fig. 2). Contour levels increase by successive factors of 1.3. 1D slices at indicated 15N chemical shifts (dashed lines in the 2D spectra) are shown in (b,d).

Dmitry S. Kryndushkin, et al. J Mol Biol. ;409(2):263-277.
4.
Figure 2

Figure 2. From: The core of Ure2p prion fibrils is formed by the N-terminal segment in a parallel cross-? structure: Evidence from solid state NMR.

2D 13C-13C NMR spectra of prion-seeded Ure2p fibrils before (a,b) and after (c,d) proteinase K treatment. Ile residues within Ure2p are uniformly 15N,13C-labeled. Spectra were obtained in a 14.1 T magnetic field. Contour levels increase by successive factors of 1.5 (a,c) or 1.3 (b,d). Dashed rectangle and arrows indicate Ile crosspeak signals that are eliminated by proteinase K treatment.

Dmitry S. Kryndushkin, et al. J Mol Biol. ;409(2):263-277.
5.
Figure 6

Figure 6. From: The core of Ure2p prion fibrils is formed by the N-terminal segment in a parallel cross-? structure: Evidence from solid state NMR.

(a) Aliphatic region of the 1D 13C NMR spectrum of prion-seeded Ure2p fibrils in which Ile residues are uniformly 15N,13C-labeled, with assignments to Ile carbon sites. (b,c) 1H-13C cross-polarization build-up data for the indicated sites (open symbols). Solid and dashed lines in (b) are data for Cα and Cβ sites in uniformly 15N,13C-labeled L-valine powder, obtained under identical experimental conditions. Solid line in (c) is data for methyl sites in uniformly 15N,13C-labeled L-valine powder.

Dmitry S. Kryndushkin, et al. J Mol Biol. ;409(2):263-277.
6.
Figure 7

Figure 7. From: The core of Ure2p prion fibrils is formed by the N-terminal segment in a parallel cross-? structure: Evidence from solid state NMR.

(a) Structural model for full-length Ure2p fibrils, generated as described in the text. A fibril section comprised of nine Ure2p dimers is shown, viewed down the fibril axis (top) and from the side (bottom). CTD dimers are shown in a cartoon representation, with each dimer in a distinct color. Residues 1-81 are shown in an all-atom representation. The fibril diameter is 20 nm, in good agreement with Fig 1c. (b) PD segments of one dimer, viewed down the fibril axis, representing a possible molecular structure for the cross-β fibril core.

Dmitry S. Kryndushkin, et al. J Mol Biol. ;409(2):263-277.
7.
Figure 5

Figure 5. From: The core of Ure2p prion fibrils is formed by the N-terminal segment in a parallel cross-? structure: Evidence from solid state NMR.

(a) 13C NMR spectrum of unseeded Ure2p fibrils in which Ile residues are 13C-labeled only at carbonyl sites. Thin lines are a fit of the carbonyl lineshape with five Gaussian components. Dashed line is the residual after fitting, offset vertically for clarity. (b) Decay of 13C NMR signals due to 13C-13C magnetic dipole-dipole couplings for the five Gaussian components (open symbols), the sum of components 1-3 (filled stars), and the sum of components 4 and 5 (filled pentagons). Data were obtained with the PITHIRDS-CT dipolar recoupling technique40. Lines are numerical simulations of PITHIRDS-CT data for linear chains of 13C nuclei with the indicated spacings. (c) 13C NMR spectrum of the same sample after proteinase K treatment. (d) PITHIRDS-CT data (filled circles) of the same sample after proteinase K treatment.

Dmitry S. Kryndushkin, et al. J Mol Biol. ;409(2):263-277.

Display Settings:

Items per page

Supplemental Content

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Write to the Help Desk