Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

19.5K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
19.5K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

2.8K
2.8K
Global Climate Change01:50

Global Climate Change

29.0K
Throughout its ~4.5 billion year history, the Earth has experienced periods of warming and cooling. However, the current drastic increase in global temperatures is well outside of the Earth’s cyclic norms, and evidence for human-caused global climate change is compelling. Paleoclimatology, the study of ancient climate conditions, provides ample evidence for human-caused global climate change by comparing recent conditions with those in the past.
29.0K
Extrinsic and Intrinsic Pathways of Hemostasis01:20

Extrinsic and Intrinsic Pathways of Hemostasis

12.9K
Blood clotting or coagulation involves extrinsic and intrinsic pathways, which ultimately merge into the common pathway, forming a fibrin clot.
The Extrinsic Pathway
The extrinsic pathway of coagulation is typically initiated by tissue damage that exposes blood to tissue factor (TF), a protein released by the damaged tissue cells outside the blood vessels—this interaction with TF triggers biochemical reactions involving specific clotting factors. The key player here is Factor VII, which...
12.9K
The Intrinsic Apoptotic Pathway01:31

The Intrinsic Apoptotic Pathway

8.6K
Internal cellular stress, such as cellular injury or hypoxia, triggers intrinsic apoptosis. The B-cell lymphoma 2 (Bcl-2) family of proteins are the primary regulators of the intrinsic apoptotic pathway. For example, during DNA damage, checkpoint proteins, such as Ataxia Telangiectasia Mutated (ATM protein) and Checkpoints Factor-2 (Chk2) proteins, are activated. These proteins phosphorylate p53 which further activates pro-apoptotic proteins, such as Bax, Bak, PUMA, and Noxa, and inhibits...
8.6K
Introduction to Global Positioning System01:30

Introduction to Global Positioning System

541
The Global Positioning System (GPS) revolutionized positioning on Earth, providing precise location data through satellite ranging. The GPS system was developed in 1978 by the U.S. Department of Defense  for military use, and it became available for civilian applications in 1983, transforming fields including navigation, fleet management, and time synchronization for telecommunications systems.GPS consists of satellites in medium Earth orbit, about 20,200 kilometers above the surface,...
541

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Tunable, High-Relaxivity Gd(III)-Conjugated Lipoic Acid Hydrogels for Magnetic Resonance Imaging.

ACS applied materials & interfaces·2026
Same author

Biomimetic Dual-Multivalent Strategy Enabled <i>In Vivo</i> Tumor-Targeted Molecular MRI.

Analytical chemistry·2026
Same author

An Enzyme-Responsive Gd(III) MRI Probe for Visualizing β-Hexosaminidase A Activity.

ACS sensors·2026
Same author

Cooperativity, dynamics, and the free-energy surfaces of charge-patterned IDPs.

bioRxiv : the preprint server for biology·2026
Same author

IFI16 restricts SARS-CoV-2 replication by disrupting nucleocapsid-driven phase separation.

Communications biology·2026
Same author

Advancements in single-molecule fluorescence spectroscopy for probing conformations, dynamics, and interactions in disordered protein regions.

Current opinion in structural biology·2026

Related Experiment Video

Updated: Feb 5, 2026

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

2.3K

Local and Global Dynamics in Intrinsically Disordered Synuclein.

Nasrollah Rezaei-Ghaleh1, Giacomo Parigi2, Andrea Soranno3,4

  • 1University Medical Center Göttingen &, German Center for Neurodegenerative Diseases (DZNE) &, MPI for Biophysical Chemistry, Von-Siebold-Strasse 3a, 37075, Göttingen, Germany.

Angewandte Chemie (International Ed. in English)
|September 6, 2018
PubMed
Summary
This summary is machine-generated.

Intrinsically disordered proteins (IDPs) exhibit complex motions. This study combines nuclear spin relaxation, nsFCS, and simulations to reveal alpha-synuclein

Keywords:
NMR spectroscopyintrinsically disordered proteinsprotein dynamics

More Related Videos

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions
08:40

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions

Published on: June 23, 2022

3.5K
Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One &#945;-Synuclein Monomer at a Time
07:56

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

Published on: May 30, 2021

3.6K

Related Experiment Videos

Last Updated: Feb 5, 2026

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

2.3K
Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions
08:40

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions

Published on: June 23, 2022

3.5K
Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One &#945;-Synuclein Monomer at a Time
07:56

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

Published on: May 30, 2021

3.6K

Area of Science:

  • Biophysics
  • Structural Biology
  • Neuroscience

Background:

  • Intrinsically disordered proteins (IDPs) lack stable tertiary structures, leading to diverse conformational dynamics.
  • Characterizing the full spectrum of IDP motions is challenging due to their inherent flexibility.
  • Alpha-synuclein, an IDP, is implicated in the pathogenesis of Parkinson disease.

Purpose of the Study:

  • To comprehensively characterize the conformational dynamics of alpha-synuclein.
  • To elucidate the role of fast and slow motions in IDP dynamics.
  • To establish a multi-technique strategy for studying residue-specific protein dynamics.

Main Methods:

  • High- and low-field nuclear spin relaxation measurements.
  • Nanosecond fluorescence correlation spectroscopy (nsFCS).
  • Long molecular dynamics simulations.

Main Results:

  • Fast motions (<2 ns) involving dihedral angle fluctuations and Ramachandran substate sampling explain N-H orientational memory loss.
  • Slow segmental dynamics (up to ~13 ns) are observed throughout the alpha-synuclein chain, particularly in the C-terminal domain.
  • Global chain reconfiguration occurs on a timescale of ~60 ns.

Conclusions:

  • A powerful multi-technique approach was demonstrated for characterizing IDP dynamics.
  • The study provides residue-specific insights into the conformational dynamics of alpha-synuclein.
  • Understanding these dynamics is crucial for deciphering the role of IDPs in disease.