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

Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...

You might also read

Related Articles

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

Sort by
Same author

Liquid-liquid phase separation enables chromatography-free purification and high-performance spidroin-amyloid hybrid silk fibers.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

A signal-responsive cooperative transcription factor network determines alveolar macrophage identity.

The Journal of experimental medicine·2026
Same author

Differential Scanning Calorimetry of Protein-Lipid Interactions.

Methods in molecular biology (Clifton, N.J.)·2026
Same author

Validity and reliability of <math><mover><mi>V</mi> <mo>˙</mo></mover></math> O<sub>2max</sub> determination immediately after a maximal fat oxidation assessment in pre-diabetes/type 2 Diabetes Mellitus population.

Sports medicine and health science·2026
Same author

Effects of a 6-Month Educational Program on Blood Pressure in Pre-Frail and Frail Older Adults: A Randomized Controlled Trial.

Healthcare (Basel, Switzerland)·2026
Same author

Response to the Letter to the Editor by Wu et al. Regarding the Article "Improvements in Depressive Symptoms, Perceived Social Support, and Quality of Life Through an Educational Program in Community-Dwelling Older Adults With Frailty Phenotype".

The American journal of geriatric psychiatry : official journal of the American Association for Geriatric Psychiatry·2026

Related Experiment Video

Updated: Jun 8, 2026

Material Formation of Recombinant Spider Silks through Aqueous Solvation using Heat and Pressure
10:26

Material Formation of Recombinant Spider Silks through Aqueous Solvation using Heat and Pressure

Published on: May 6, 2019

A pH-dependent dimer lock in spider silk protein.

Michael Landreh1, Glareh Askarieh, Kerstin Nordling

  • 1Division of Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-171 77 Stockholm, Sweden.

Journal of Molecular Biology
|October 5, 2010
PubMed
Summary

Spider silk proteins (spidroins) use pH changes to assemble. Lowering pH below 6.4 stabilizes the N-terminal domain, promoting spider silk formation through electrostatic interactions.

More Related Videos

Synthetic Spider Silk Production on a Laboratory Scale
13:36

Synthetic Spider Silk Production on a Laboratory Scale

Published on: July 18, 2012

Related Experiment Videos

Last Updated: Jun 8, 2026

Material Formation of Recombinant Spider Silks through Aqueous Solvation using Heat and Pressure
10:26

Material Formation of Recombinant Spider Silks through Aqueous Solvation using Heat and Pressure

Published on: May 6, 2019

Synthetic Spider Silk Production on a Laboratory Scale
13:36

Synthetic Spider Silk Production on a Laboratory Scale

Published on: July 18, 2012

Area of Science:

  • Biochemistry
  • Materials Science
  • Structural Biology

Background:

  • Spider dragline silk is a natural polymer known for its exceptional strength.
  • It is primarily composed of major ampullate spidroin (MaSp) proteins.
  • The N-terminal (NT) domain of MaSp1 plays a crucial role in spidroin assembly.

Purpose of the Study:

  • To investigate the pH-dependent mechanism of spidroin assembly.
  • To understand the structural changes in the MaSp1 NT domain at different pH levels.
  • To identify the key residues involved in pH-sensitive interactions.

Main Methods:

  • Amide hydrogen/deuterium exchange mass spectrometry (DXMS) to detect structural changes.
  • Nondenaturing electrospray ionization mass spectrometry (ESI-MS) to analyze protein interactions.
  • Analytical ultracentrifugation to confirm dimerization.

Main Results:

  • Global structural stabilization of the MaSp1 NT domain was observed at low pH (<6.4).
  • This stabilization is dependent on electrostatic interactions involving Asp40 and Glu84 residues.
  • Dimerization of the NT domain was detected in the gas phase at low pH, suggesting a key step in aggregation.

Conclusions:

  • The study elucidates a pH-sensitive mechanism for spider silk assembly.
  • Lowering pH induces structural changes and electrostatic interactions in the spidroin NT domain.
  • This process locks spidroin NT dimers, facilitating spider silk formation.