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 Complex Assembly02:41

Protein Complex Assembly

17.1K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
17.1K
Protein Complex Assembly02:41

Protein Complex Assembly

2.7K
2.7K
Protein-protein Interfaces02:04

Protein-protein Interfaces

15.0K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
15.0K
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

5.9K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
5.9K
Ligand Binding Sites02:40

Ligand Binding Sites

15.7K
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...
15.7K
Protein and Protein Structure02:15

Protein and Protein Structure

92.0K
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...
92.0K

You might also read

Related Articles

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

Sort by
Same author

Probing molecular diversity and ultrastructure of brain cells with fluorescent aptamers.

Nature communications·2026
Same author

Multiomics characterization of acute child illness and mortality in Africa and South Asia.

Nature communications·2026
Same author

Safety and efficacy of CRS3123 in adults with a primary episode or first recurrence of Clostridioides difficile infection: a phase 2, randomised, double-blind, multicentre, vancomycin-controlled study.

The Lancet. Infectious diseases·2026
Same author

Proteomic profiles in the aqueous following anti-vegf therapy in treatment naïve neovascular age-related macular degeneration.

Clinical proteomics·2025
Same author

Activated GDF11/8 subforms predict cardiovascular events and mortality in humans.

Nature communications·2025
Same author

Hospital Mortality in Acute Decompensation of Alcoholic Liver Cirrhosis: Can Novel Survival Markers Outperform Traditional Ones?

Journal of clinical medicine·2024

Related Experiment Video

Updated: Mar 25, 2026

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis
08:09

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis

Published on: January 7, 2017

11.4K

Embracing proteins: structural themes in aptamer-protein complexes.

Amy D Gelinas1, Douglas R Davies2, Nebojsa Janjic1

  • 1SomaLogic, Inc., 2945 Wilderness Place, Boulder, CO 80301, United States.

Current Opinion in Structural Biology
|February 27, 2016
PubMed
Summary
This summary is machine-generated.

Aptamers fold into precise 3D structures for high-affinity protein binding, revealing emerging trends in their structural rules. Novel motifs in modified aptamers are crucial for function, similar to antibodies in recognizing protein epitopes.

More Related Videos

Primer-Free Aptamer Selection Using A Random DNA Library
11:14

Primer-Free Aptamer Selection Using A Random DNA Library

Published on: July 26, 2010

25.6K
Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
11:34

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Published on: August 9, 2019

7.2K

Related Experiment Videos

Last Updated: Mar 25, 2026

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis
08:09

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis

Published on: January 7, 2017

11.4K
Primer-Free Aptamer Selection Using A Random DNA Library
11:14

Primer-Free Aptamer Selection Using A Random DNA Library

Published on: July 26, 2010

25.6K
Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
11:34

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Published on: August 9, 2019

7.2K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Aptamers are increasingly used as affinity reagents in various applications.
  • Understanding aptamer-protein interactions is crucial for optimizing their use.
  • Current knowledge is based on a limited number of available aptamer-protein structures.

Purpose of the Study:

  • To analyze emerging trends in the structural rules governing aptamer-protein interactions.
  • To identify key structural features that enable specific, high-affinity binding.
  • To compare aptamer binding strategies with those of other affinity reagents like antibodies.

Main Methods:

  • Analysis of existing aptamer-protein complex structures (16 available).
  • Identification of common and novel structural motifs.
  • Comparison of structural features with antibody-protein interactions.

Main Results:

  • Aptamers utilize their flexible phosphodiester backbone to form precise 3D structures.
  • Known nucleic acid motifs serve as scaffolds for orienting functional groups.
  • Modified aptamers with diversity-enhancing side chains exhibit novel motifs essential for function.
  • Aptamers and antibodies recognize protein epitopes of similar size and shape complementarity.

Conclusions:

  • Emerging structural trends provide insights into aptamer-protein binding.
  • Both conserved and novel structural motifs contribute to aptamer efficacy.
  • Aptamers offer an alternative to antibodies as affinity reagents, with comparable binding capabilities.