Journal
/
Biochemistry
/
High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
JoVE Journal
Biochemistry
A subscription to JoVE is required to view this content.  Sign in or start your free trial.
JoVE Journal Biochemistry
High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

DOI:
10.3791/63664-v

•

08:48 min

•

April 28, 2022

•

, , , , , , ,
1Institut für Angewandte Physik,Universität Tübingen, 2Institut Max von Laue – Paul Langevin (ILL), 3Institut de Biologie Structurale,Université Grenoble Alpes, 4Institut Européen de Chimie et Biologie, Bordeaux INP, Chimie et Biologie des Membranes et des Nanoobjets (CBMN),Université de Bordeaux

Chapters

  • 00:04Introduction
  • 01:04Preparation of H2O‐Hydrated Powders of Perdeuterated Protein
  • 03:14Incoherent Neutron Scattering Experiment
  • 06:57Results: Dynamics of Proteins and Hydration Water
  • 07:57Conclusion

Summary

Automatic Translation

Automatic Translation

Neutron backscattering spectroscopy offers a nondestructive and label-free access to the ps-ns dynamics of proteins and their hydration water. The workflow is presented with two studies on amyloid proteins: on the time-resolved dynamics of lysozyme during aggregation and on the hydration water dynamics of tau upon fiber formation.

Tags

Keywords: Neutron BackscatteringNeutron SpectroscopyProtein DynamicsHydration WaterPicosecond-nanosecond TimescaleAlzheimer’sParkinson’sSample PreparationHydrogen-deuterium Exchange

Article

Embed

ADD TO PLAYLIST

Usage Statistics

Related Videos

check_url/63664?article_type=v

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
check_url/63664?article_type=v

Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications
check_url/63664?article_type=v

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
check_url/63664?article_type=v

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)
check_url/63664?article_type=v

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
check_url/63664?article_type=v

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis
check_url/63664?article_type=v

An Integrated Raman Spectroscopy and Mass Spectrometry Platform to Study Single-Cell Drug Uptake, Metabolism, and Effects
check_url/63664?article_type=v

Transverse Sectioning of Mature Rice (Oryza sativa L.) Kernels for Scanning Electron Microscopy Imaging Using Pipette Tips as Immobilization Support
check_url/63664?article_type=v

Dual-Color Fluorescence Cross-Correlation Spectroscopy to Study Protein-Protein Interaction and Protein Dynamics in Live Cells
check_url/63664?article_type=v

CD Spectroscopy to Study DNA-Protein Interactions

Read Article