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

Amyloid Fibrils03:03

Amyloid Fibrils

9.9K
Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
9.9K
Protein Folding01:25

Protein Folding

8.8K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
8.8K
Amides to Carboxylic Acids: Hydrolysis01:28

Amides to Carboxylic Acids: Hydrolysis

3.5K
Amides can undergo either acid-catalyzed hydrolysis or base-promoted hydrolysis through a typical nucleophilic acyl substitution. Each hydrolysis requires severe conditions.
Acid-catalyzed hydrolysis:
Hydrolysis of amides under acidic conditions yields carboxylic acids. Since the reaction occurs slowly, hydrolysis requires the conditions of heat.
The mechanism begins with the protonation of the carbonyl oxygen by the acid catalyst. The protonation makes the amide carbonyl carbon more...
3.5K
Lysosomal Hydrolases01:22

Lysosomal Hydrolases

3.9K
Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
3.9K
Ligand Binding Sites02:40

Ligand Binding Sites

13.5K
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
13.5K
Amino acids03:42

Amino acids

91.9K
Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible...
91.9K

You might also read

Related Articles

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

Sort by
Same author

Evolution of the ribosomal exit tunnel through the eyes of the nascent chain.

Nucleic acids research·2026
Same author

Structures of protein folding intermediates on the ribosome.

Nature structural & molecular biology·2026
Same author

Small Molecule Activators of Protein Phosphatase 2A Exert Global Stabilizing Effects on the Scaffold PR65.

JACS Au·2026
Same author

Transient tertiary structure in intrinsically disordered proteins revealed by multithermal enhanced sampling.

Nature communications·2026
Same author

Microscopy-based techniques for studying the material properties of biomolecular condensates in the cellular environment.

Biophysical reviews·2025
Same author

Affinity-selected peptide ligands specifically bind i-motif DNA and modulate c-Myc gene expression.

Nucleic acids research·2025
Same journal

Overcoming the Catalytic Bucket Effect in Pt-based High-Entropy Nanocages Through Interface Defect and Strain Engineering.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same journal

Rare-Earth-Sulfur Surface Modification Enables SiC Ceramics for Low-Frequency Electromagnetic Wave Absorption in Extreme Environments.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same journal

PFKFB4 Deubiquitination by USP10 Enhances Fumarate Metabolism to Orchestrate the KDM1A/Rad51 Axis and Confer Radioresistance in Lung Cancer.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same journal

Assessing Strengths and Limitations of Magnetoencephalography Source Imaging With Intracerebral EEG.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same journal

Efficient Adsorption-Based Direct Air Capture Via Triply Periodic Minimal Surface Architectures.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same journal

Inhalable ROS-Responsive Nanospray Activates PPAR-γ to Restore Macrophage Mitochondrial Homeostasis and Attenuate Radiation-Induced Lung Injury.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
See all related articles

Related Experiment Video

Updated: Sep 18, 2025

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

6.3K

Amyloid Forming Human Lysozyme Intermediates are Stabilized by Non-Native Amide-π Interactions.

Minkoo Ahn1,2,3, Julian O Streit2, Christopher A Waudby2,4

  • 1School of Biochemistry, University of Bristol, University Walk, Bristol, BS8 1TD, UK.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)
|June 25, 2025
PubMed
Summary
This summary is machine-generated.

Researchers investigated a transient intermediate state in human lysozyme amyloidosis using NMR and simulations. This study reveals structural insights into the intermediate, crucial for understanding and targeting this fatal hereditary disease.

Keywords:
CEST NMRMD simulationsamide‐π interactionsamyloidhuman lysozymeprotein intermediate

More Related Videos

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
08:53

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Published on: March 21, 2025

871
High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
08:48

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

Published on: April 28, 2022

1.9K

Related Experiment Videos

Last Updated: Sep 18, 2025

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

6.3K
Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
08:53

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Published on: March 21, 2025

871
High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
08:48

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

Published on: April 28, 2022

1.9K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Human lysozyme variants can cause fatal hereditary systemic amyloidosis.
  • Amyloid formation involves a transient intermediate state that is difficult to study structurally.

Purpose of the Study:

  • To investigate the structure and properties of the transient intermediate state in an amyloid-forming human lysozyme variant (I59T).
  • To gain insights into the mechanism of lysozyme amyloidosis for potential therapeutic targeting.

Main Methods:

  • Utilized Chemical Exchange Saturation Transfer (CEST) and Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion Nuclear Magnetic Resonance (NMR) spectroscopy at low pH.
  • Employed molecular dynamics (MD) simulations to model the folding pathway and free energy landscape.

Main Results:

  • Identified and characterized a distinct intermediate state populated at 0.6% during thermal unfolding using 15N CEST and CPMG RD NMR.
  • Observed unusual 1H chemical shifts in the intermediate state, confirmed by 1H CEST.
  • MD simulations recapitulated the experimental findings, revealing a high-energy intermediate with a disordered beta-domain and C-helix stabilized by non-native interactions.

Conclusions:

  • Provided the first direct structural information on the transient intermediate state of amyloid-forming human lysozyme.
  • Elucidated the structural features stabilizing the intermediate, including non-native hydrogen bonding and amide-pi interactions.
  • Offered critical insights into the molecular mechanisms underlying lysozyme amyloidosis, potentially guiding therapeutic strategies.