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Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Feedback Regulation of Calcium Concentration01:27

Feedback Regulation of Calcium Concentration

Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Free Energy Changes for Nonstandard States03:25

Free Energy Changes for Nonstandard States

The free energy change for a process taking place with reactants and products present under nonstandard conditions (pressures other than 1 bar; concentrations other than 1 M) is related to the standard free energy change according to this equation:
Crystal Field Theory - Octahedral Complexes02:58

Crystal Field Theory - Octahedral Complexes

Crystal Field Theory
To explain the observed behavior of transition metal complexes (such as colors), a model involving electrostatic interactions between the electrons from the ligands and the electrons in the unhybridized d orbitals of the central metal atom has been developed. This electrostatic model is crystal field theory (CFT). It helps to understand, interpret, and predict the colors, magnetic behavior, and some structures of coordination compounds of transition metals.
CFT focuses on...
Positive Regulator Molecules01:45

Positive Regulator Molecules

To consistently produce healthy cells, the cell cycle—the process that generates daughter cells—must be precisely regulated.

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Related Experiment Video

Updated: May 18, 2026

Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

Functional Calmodulin States Are Selected from an Electrostatically Tuned Free Energy Landscape.

Busra Tayhan1, Sila Horozoglu1, Ali Rana Atilgan1

  • 1Faculty of Engineering and Natural Sciences, Sabanci University, Tuzla, Istanbul 34956, Türkiye.

Journal of Chemical Information and Modeling
|May 16, 2026
PubMed
Summary

Calmodulin (CaM) protein dynamics were simulated to understand its conformational changes. Calcium binding and salt concentration significantly influence CaM

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Area of Science:

  • Molecular Biology
  • Biophysics
  • Computational Chemistry

Background:

  • Calmodulin (CaM) is a crucial calcium-binding protein regulating numerous cellular processes.
  • CaM's structural flexibility allows it to interact with diverse targets, but its full conformational landscape is difficult to characterize.
  • Understanding CaM's conformational dynamics is key to deciphering its role in cellular signaling.

Purpose of the Study:

  • To explore the conformational landscape of calcium-bound and calcium-free calmodulin.
  • To investigate the effects of physiological and low salt concentrations on CaM conformations.
  • To elucidate how calcium and ionic strength orchestrate CaM's dynamic behavior.

Main Methods:

  • Well-tempered metadynamics simulations were performed.
  • Physically interpretable collective variables were utilized to enhance sampling.
  • Simulations were conducted under varying calcium and salt conditions.

Main Results:

  • Four principal CaM conformations were identified, with populations varying based on calcium binding and ionic strength.
  • Calcium binding promotes compact CaM states.
  • Low salt conditions facilitate transitions but can lead to kinetic trapping via salt-bridge interactions.

Conclusions:

  • Calcium and ionic strength are critical regulators of CaM's conformational ensemble.
  • Target binding stabilizes extended CaM conformations, distinct from those accessible to free CaM.
  • These findings provide insights into the mechanisms underlying CaM's role in cellular signaling.