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

Affinity and Avidity01:41

Affinity and Avidity

39.0K
Overview
39.0K
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

15.0K
The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
15.0K
Electron Affinity03:07

Electron Affinity

43.3K
The electron affinity (EA) is the energy change for adding an electron to a gaseous atom to form an anion (negative ion).
43.3K
Habitat Fragmentation02:31

Habitat Fragmentation

21.4K
Habitat fragmentation describes the division of a more extensive, continuous habitat into smaller, discontinuous areas. Human activities such as land conversion, as well as slower geological processes leading to changes in the physical environment, are the two leading causes of habitat fragmentation. The fragmentation process typically follows the same steps: perforation, dissection, fragmentation, shrinkage, and attrition.
21.4K
Peptide Bonds02:43

Peptide Bonds

82.9K
A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
82.9K
Factors Affecting Protein-Drug Binding: Protein-Related Factors01:20

Factors Affecting Protein-Drug Binding: Protein-Related Factors

558
Drug binding to proteins is a key aspect of pharmacokinetics and can influence a drug's distribution, absorption, and elimination in the body. Several factors, including the drug's physiochemical properties, protein concentration, disease states, and the number of binding sites on the protein, influence this process.
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be...
558

You might also read

Related Articles

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

Sort by
Same author

Retargeted adenoviruses for local IgA and CD47 blocker production as a novel cancer therapy.

EMBO molecular medicine·2026
Same author

Semi-automated Ribosome Display for High-Throughput DARPin Binder Selection.

New biotechnology·2026
Same author

Computational design of a soluble mimic of the outer membrane LPS transport protein LptD suitable for screening of antibiotics.

Protein science : a publication of the Protein Society·2026
Same author

Transcriptional transactivation turns human iPSC-derived macrophages into an adenovirus-producing cell state.

Journal of virology·2026
Same author

DARPins as pan-reactivators of temperature-sensitive p53 cancer mutants.

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

Cryo-EM structures of higher order Gephyrin oligomers reveal principles of inhibitory postsynaptic scaffold organization.

Nature communications·2026

Related Experiment Video

Updated: Feb 1, 2026

Protein Purification-free Method of Binding Affinity Determination by Microscale Thermophoresis
10:22

Protein Purification-free Method of Binding Affinity Determination by Microscale Thermophoresis

Published on: August 15, 2013

31.3K

Peptide binding affinity redistributes preassembled repeat protein fragments.

Erich Michel1, Andreas Plückthun2, Oliver Zerbe1

  • 1Department of Chemistry, University of Zurich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland.

Biological Chemistry
|December 6, 2018
PubMed
Summary
This summary is machine-generated.

Designed armadillo repeat proteins (dArmRPs) can self-assemble into functional binders. Peptide binding induces conformational changes and allows enrichment of the strongest binders from mixed fragments.

Keywords:
NMR spectroscopypeptide bindingprotein designprotein fragment complementationrepeat protein

More Related Videos

Comparing the Affinity of GTPase-binding Proteins using Competition Assays
10:37

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Published on: October 8, 2015

9.6K
Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
14:58

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

Published on: November 12, 2012

48.8K

Related Experiment Videos

Last Updated: Feb 1, 2026

Protein Purification-free Method of Binding Affinity Determination by Microscale Thermophoresis
10:22

Protein Purification-free Method of Binding Affinity Determination by Microscale Thermophoresis

Published on: August 15, 2013

31.3K
Comparing the Affinity of GTPase-binding Proteins using Competition Assays
10:37

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Published on: October 8, 2015

9.6K
Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
14:58

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

Published on: November 12, 2012

48.8K

Area of Science:

  • Protein engineering
  • Biochemistry
  • Molecular recognition

Background:

  • Designed armadillo repeat proteins (dArmRPs) are modular protein binders.
  • dArmRPs consist of capping repeats (Y, A) and internal modules (M) recognizing specific peptide sequences.
  • Previous work showed peptide-guided assembly of dArmRP fragments split within internal modules.

Purpose of the Study:

  • Investigate spontaneous assembly of dArmRP fragments from inter-module splits.
  • Explore peptide-induced conformational changes in assembled dArmRP fragments.
  • Assess the feasibility of peptide-induced enrichment of high-affinity binders from fragment mixtures.

Main Methods:

  • Studied dArmRP fragments that spontaneously assemble with high affinity.
  • Analyzed peptide-induced distal conformational rearrangements using population analysis.
  • Examined equimolar mixtures of N- and C-terminal fragments with varying peptide affinities.

Main Results:

  • Certain dArmRP fragments assemble spontaneously with high affinity.
  • Peptide binding induces global conformational changes, suggesting induced fit.
  • A mixture of fragments showed initial assembly of the weakest binder.
  • Addition of target peptide shifted the population towards the highest-affinity binder, especially with excess peptide.

Conclusions:

  • Spontaneously assembling dArmRP fragments can undergo peptide-induced conformational changes.
  • Peptide-induced enrichment of best binders from inter-modular fragment mixtures is feasible.
  • This demonstrates a strategy for selecting high-affinity protein binders through peptide interaction.