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

Proofreading01:31

Proofreading

Synthesis of new DNA molecules is carried out by the enzyme DNA polymerase, which adds nucleotides on the daughter strand complementary to the template DNA strand. DNA polymerase has a higher affinity to add the correct base and ensures fidelity during DNA replication. Furthermore,  it exhibits proofreading activity during replication, using an exonuclease domain that cuts off incorrect nucleotides from the nascent DNA strand.
Errors During Replication are Corrected by the DNA Polymerase Enzyme
Proofreading01:43

Proofreading

Overview
PCR - Polymerase Chain Reaction01:32

PCR - Polymerase Chain Reaction

Overview
PCR01:32

PCR

Overview
Actin Polymerization01:42

Actin Polymerization

Actin polymerization occurs through the head-to-tail association of binding sites on monomeric actin or G-actin to form filamentous or F-actin. The polymerization can be divided into three phases ̶  nucleation, elongation, and steady-state phase.
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight actin...
Translesion DNA Polymerases02:10

Translesion DNA Polymerases

Translesion (TLS) polymerases rescue stalled DNA polymerases at sites of damaged bases by replacing the replicative polymerase and installing a nucleotide across the damaged site. Doing so, TLS allows additional time for the cell to repair the damage before resuming regular DNA replication.
TLS polymerases are found in all three domains of life - archaea, bacteria, and eukaryotes. Of the different classes of TLS polymerases, members of the Y family are fitted with specialized structures that...

You might also read

Related Articles

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

Sort by
Same author

How much Copper Do Calves Need? Retention and Hepatic Storage in Artificially Reared Milk-Fed Holstein-Friesian Calves.

Biological trace element research·2026
Same author

Association between dog ownership and mental health among community-dwelling older adults: a cross-sectional study.

Frontiers in public health·2026
Same author

Reply to Jin and Xu: "Distinct Associations of Apathy and Depressive Symptoms With Multidimensional Frailty: Methodological Considerations and Future Directions".

Geriatrics & gerontology international·2026
Same author

Prothrombinase processivity is conferred by substrate allostery.

The EMBO journal·2026
Same author

Associations of Apathy and Depressive Symptoms With Frailty Domains in Individuals Aged 75 Years Old: A Cross-Sectional Study.

Geriatrics & gerontology international·2026
Same author

Reliability and Validity of the Japanese Version of the eHealth Literacy Scale in Community-Dwelling Older Adults: A Cross-Sectional Study.

European journal of investigation in health, psychology and education·2026
Same journal

1,2-Aminothiol-specific conjugation for dual-color fluorescent labeling via ultrafast TAMM conjugates.

Methods in enzymology·2026
Same journal

Nitrone dipoles in bioorthogonal chemistry applications.

Methods in enzymology·2026
Same journal

Bioorthogonal labeling of sialic acid isomers for detection of glycoconjugates by mass spectrometry imaging and microscopy.

Methods in enzymology·2026
Same journal

Bioorthogonal photocatalytic proximity labeling for quantitative mapping of cell-cell interactions.

Methods in enzymology·2026
Same journal

inCu-click: Enabling copper-catalyzed click chemistry inside living cells.

Methods in enzymology·2026
Same journal

Site-specific antibody labeling via endo-S2 mediated Fc glycan remodeling.

Methods in enzymology·2026
See all related articles

Related Experiment Video

Updated: May 27, 2026

Designed for Molecular Recycling: A Lignin-Derived Semi-aromatic Biobased Polymer
10:22

Designed for Molecular Recycling: A Lignin-Derived Semi-aromatic Biobased Polymer

Published on: November 30, 2020

Serpin polymerization in vitro.

James A Huntington1, Masayuki Yamasaki

  • 1Department of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.

Methods in Enzymology
|November 15, 2011
PubMed
Summary
This summary is machine-generated.

Serpin polymerization, often caused by mutations, can be studied in vitro. New research explores polymerization mechanisms, including the loop-sheet hypothesis and domain swaps, to understand misfolded serpin states.

More Related Videos

DNA Polymerase Activity Assay Using Near-infrared Fluorescent Labeled DNA Visualized by Acrylamide Gel Electrophoresis
07:38

DNA Polymerase Activity Assay Using Near-infrared Fluorescent Labeled DNA Visualized by Acrylamide Gel Electrophoresis

Published on: October 6, 2017

Strand-Specific Analysis of Proteins at Replicating DNA Strands by Enrichment and Sequencing of Protein-Associated Nascent DNA Method
08:53

Strand-Specific Analysis of Proteins at Replicating DNA Strands by Enrichment and Sequencing of Protein-Associated Nascent DNA Method

Published on: May 2, 2025

Related Experiment Videos

Last Updated: May 27, 2026

Designed for Molecular Recycling: A Lignin-Derived Semi-aromatic Biobased Polymer
10:22

Designed for Molecular Recycling: A Lignin-Derived Semi-aromatic Biobased Polymer

Published on: November 30, 2020

DNA Polymerase Activity Assay Using Near-infrared Fluorescent Labeled DNA Visualized by Acrylamide Gel Electrophoresis
07:38

DNA Polymerase Activity Assay Using Near-infrared Fluorescent Labeled DNA Visualized by Acrylamide Gel Electrophoresis

Published on: October 6, 2017

Strand-Specific Analysis of Proteins at Replicating DNA Strands by Enrichment and Sequencing of Protein-Associated Nascent DNA Method
08:53

Strand-Specific Analysis of Proteins at Replicating DNA Strands by Enrichment and Sequencing of Protein-Associated Nascent DNA Method

Published on: May 2, 2025

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Serpin polymerization occurs in vivo due to folding defects from point mutations.
  • In vitro methods are crucial for studying serpin polymer formation and molecular basis.
  • Previous research focused on the "loop-sheet" hypothesis for polymer formation.

Purpose of the Study:

  • To outline techniques for producing and characterizing serpin polymerization in vitro.
  • To discuss findings in light of current polymerization models.
  • To encourage further research differentiating polymerization mechanisms.

Main Methods:

  • In vitro production of serpin polymers.
  • Characterization of serpin polymerization.
  • Analysis of serpin structures and existing literature.

Main Results:

  • The "loop-sheet" hypothesis explains polymer formation via reactive center loop incorporation.
  • Recent crystal structures reveal potential for larger "domain swaps" in serpin polymerization.
  • Two models, loop-sheet and domain swapping, currently explain serpin polymerization.

Conclusions:

  • In vitro techniques are essential for understanding serpin polymerization.
  • Both loop-sheet and domain-swap mechanisms may contribute to serpin polymer formation.
  • Further experiments are needed to distinguish between proposed polymerization mechanisms.