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 Experiment Videos

Ligand-dependent aggregation and cooperativity: a critique.

H A Saroff1

  • 1Laboratory of Biochemical Pharmacology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland 20892.

Biochemistry
|October 22, 1991
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Fabrication and evaluation of membranes as specific electrodes for calcium ions.

Biophysical journal·2009
Same author

The legacies of Langmuir, Ising, and Pauling: ligand binding and the helix-coil transition.

Biopolymers·1999
Same author

From glycine to glutamic acid: analysis of the proton-binding isotherm of glutamic acid.

Analytical biochemistry·1998
Same author

Analysis of the binding of ligands to large numbers of sites: the binding of tryptophan to the 11 sites of the trp RNA-binding attenuation protein.

Analytical biochemistry·1997
Same author

The multiple origins of cooperativity in binding to multi-site lattices.

FEBS letters·1996
Same author

Energetics of protein-DNA interactions: an exact calculation for binding of ligands to a lattice of overlapping sites.

Biopolymers·1995

Aggregation processes can lead to ligand-dependent cooperativity in chemical reactions. This study details how interactions within aggregates, distinct from monomer binding, contribute to observed cooperativity, requiring specific models for analysis.

Area of Science:

  • Biochemistry
  • Chemical Kinetics
  • Molecular Interactions

Background:

  • Cooperativity in chemical reactions is often explained by ligand-dependent site-site interactions.
  • Understanding these interactions, especially in aggregating systems, requires models for ligand binding to both monomers and aggregates.

Purpose of the Study:

  • To detail the mechanisms by which aggregation generates ligand-dependent cooperativity.
  • To distinguish between free energy differences in monomer-aggregate binding and ligand-dependent interactions within aggregates.

Main Methods:

  • Analysis of free energy differences contributing to cooperativity in aggregation reactions.
  • Distinction between experimentally accessible binding constants and model-derived constants.
  • Employment of an explicit assumption relating monomer and aggregate ligand binding constants under non-interactive conditions.

Related Experiment Videos

Main Results:

  • Aggregation processes can yield ligand-dependent cooperativity.
  • Two distinct free energy differences contribute to cooperativity: monomer-aggregate binding and intra-aggregate interactions.
  • Model assumptions are necessary to evaluate interaction energies from experimental aggregation data.

Conclusions:

  • Ligand-dependent cooperativity arises from aggregation processes.
  • Understanding cooperativity requires distinguishing binding affinities and interaction energies.
  • Explicit assumptions are crucial for interpreting experimental data on ligand binding in aggregating systems.