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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...
Smooth Muscle Contraction01:25

Smooth Muscle Contraction

Smooth muscle contraction is a complex process vital for various bodily functions, from maintaining blood vessel tension to facilitating the movement of food through the digestive tract. Unlike striated muscles, smooth muscle contraction begins more slowly and lasts longer.
The onset of contraction is triggered by an increase in calcium ions within the sarcoplasm, similar to the process in striated muscle. However, smooth muscles have a relatively smaller reservoir of the sarcoplasmic...
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...

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Related Experiment Video

Updated: May 24, 2026

Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

Calcium-induced changes in calmodulin structural dynamics and thermodynamics.

Guangrong Wu1, Zhengya Gao, Aichun Dong

  • 1Department of Chemistry, Fudan University, Shanghai 200433 China.

International Journal of Biological Macromolecules
|March 6, 2012
PubMed
Summary
This summary is machine-generated.

Calcium binding significantly alters calmodulin (CaM) structure and stability. Isothermal titration calorimetry and spectroscopy reveal Ca(2+)-induced conformational changes and differential stability between apo- and holo-CaM.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Calmodulin (CaM) is a crucial calcium-binding protein involved in numerous cellular signaling pathways.
  • Understanding the structural and thermodynamic basis of Ca(2+) binding to CaM is essential for elucidating its regulatory mechanisms.

Purpose of the Study:

  • To investigate the thermodynamic and structural dynamics of Ca(2+) interaction with CaM.
  • To determine the stability differences between Ca(2+)-free (apo) and Ca(2+)-bound (holo) CaM.
  • To explore Ca(2+)-induced conformational changes in CaM.

Main Methods:

  • Isothermal titration calorimetry (ITC) for thermodynamic analysis.
  • Spectroscopic methods for monitoring chemical denaturation and protein stability.
  • Amide hydrogen-deuterium (H-D) exchange coupled with Fourier transform infrared (FT-IR) spectroscopy for structural dynamics.

Main Results:

  • Ca(2+) binding induces significant conformational changes in CaM.
  • Holo-CaM exhibits greater overall conformational stability than apo-CaM.
  • Specific regions, likely EF-hand domains, show increased solvent exposure and faster H-D exchange in holo-CaM.

Conclusions:

  • Ca(2+) binding to CaM involves substantial structural rearrangements and thermodynamic contributions.
  • ITC offers a novel approach for site-specific Ca(2+) binding analysis and cooperativity estimation in CaM.
  • The study provides insights into the coupled conformational changes governing CaM function.