Structure of amyloid fibrils of the HET-s (218-289) prion as seen by solid-state NMR / Beat H. Meier.

Format:

Video

Author/Creator:

Meier, Beat H., author.

Language:

English

Subjects (All):

Amyloid--Periodicals.

Amyloid.

Amyloidosis.

Physical Description:

1 videorecording (33 min., 13 sec.)

Other Title:

Structure of amyloid fibrils of the HET-s

Place of Publication:

London : Henry Stewart Talks Ltd, 2008.

System Details:

video file

Summary:

Audio-visual presentation: 3D structure is important -- Prion hypothesis -- Prions can form amyloids -- Amyloids -- Cross-beta arrangements give characteristic fiber diffraction patterns -- Solid-state NMR can characterize amyloid fibrils -- Atomic-resolution structure determination by NMR and x-ray -- Distance information in NMR correlation spectra -- The methodology to obtain 3D structures from solid (microcrystalline) samples has recently been developed -- Structure determination is possible -- Nevertheless, amyloids are different -- Isotopic labeling allows to disentangle the intra/inter problem -- HET-s: a functional prion -- Structural information about HET-s (218-289) from earlier measurements -- Chemical shift assignment -- To go further we need distance restraints -- Distance restraints for protein fibrils -- Intramolecular restraints -- Structure calculation -- Structural features of the fibrils -- Comparison with globular proteins.

Contents:

Introduction

Topics

Prion hypothesis

Prions can form amyloids

Amyloids (1)

Amyloids (2)

Amyloids (3)

Characteristic fiber diffraction patterns

Solid-state NMR can characterize amyloid fibrils

Structure determination by NMR and X-ray

Distance info in NMR correlation spectra

Obtaining sufficient resolution in solid state

Atomic-resolution structure determination by NMR

Obtain 3D structures from solid samples

Several protein structures solved de novo by NMR

Heterogeneous samples can not give narrow lines

Heterogeneous samples can give narrow lines

Comparison of carbon spectra

Structure determination possible

Nevertheless amyloids are different

Isotopic labelling allows to disentangle the problem

HET-s: a functional prion

The flexible tail forms fibrils

Structural information about HET-s (218-289) (1)

Structural information about HET-s (218-289) (2)

Chemical shift assignment

To go further, we need distance restraints

Distance restraints for protein fibrils

Intramolecular restraints (1)

Intramolecular restraints (2)

Structure calculation

Structural features of the fibrils

Fibrils contain a triangular hydrophobic core

HET-s(218-289) (1)

Overall shape and hydrophobic core

Structure stabilized by

Structure explains NMR spectra

Hydrogen bonds

HET-s(218-289) (2)

Comparison with globular proteins

Outlook

Acknowledgement.

Notes:

Description based on: online resource; title from PDF information screen (Henry Stewart Talks Business & Management Collection, viewed April 8, 2024).

Retrieved April 10, 2024, from https://hstalks.com/bs/965/.