Journal
/
Bioquímica
/
Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
JoVE Journal
Bioquímica
É necessária uma assinatura da JoVE para visualizar este conteúdo.  Faça login ou comece sua avaliação gratuita.
JoVE Journal Bioquímica
Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

DOI:
10.3791/60108-v

•

12:58 min

•

September 12, 2019

•

, , , ,
1Centre for Misfolding Diseases, Department of Chemistry,University of Cambridge, 2Institute of Biotechnology, Life Sciences Center,Vilnius University, 3Cavendish Laboratory, Department of Physics,University of Cambridge

Capítulos

  • 00:04Título
  • 01:09Atomic Force Microscopy (AFM) Protein Aggregate Morphology Imaging
  • 05:09Infrared (IR) Nanospectroscopy Protein Aggregate Measurement
  • 11:57Results: Individual Protein Aggregated Characterization by IR Nanospectroscopy and AFM
  • 13:30Conclusion

Summary

Tadução automática

Tadução automática

We describe the application of infrared nanospectroscopy and high-resolution atomic force microscopy to visualize the process of protein self-assembly into oligomeric aggregates and amyloid fibrils, which is closely associated with the onset and development of a wide range of human neurodegenerative disorders.

Tags

Protein AggregatesInfrared NanospectroscopyAtomic Force MicroscopySingle Molecule MethodsBiomolecular ProcessesNano ScaleHeterogeneous SystemsProtein AggregationBiomaterialsDrug DeliveryAFM ParametersAFM ImagingAFM CantileverAFM Laser BeamAFM Deflected BeamAFM OscillationAFM Resonance

Article

Embed

ADICIONAR À PLAYLIST

Usage Statistics

Vídeos Relacionados

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Enrichment of Detergent-insoluble Protein Aggregates from Human Postmortem Brain

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

High Sensitivity Measurement of Transcription Factor-DNA Binding Affinities by Competitive Titration Using Fluorescence Microscopy

Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Imaging of Extracellular Vesicles by Atomic Force Microscopy

Read Article