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

G-protein Coupled Receptors01:21

G-protein Coupled Receptors

131.6K
G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
131.6K
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

16.6K
G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
16.6K
Quantifying Agonist Activity at G Protein-coupled Receptors11:45

Quantifying Agonist Activity at G Protein-coupled Receptors

19.8K
A method for estimating the affinity constant of an agonist for the active state (Kb) of a G protein-coupled receptor is described. The analysis provides absolute or relative measures of Kb depending on whether constitutive receptor activation is measurable. Our method applies to various responses downstream from receptor...
19.8K
Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors16:16

Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors

15.7K
We genetically-encode the unnatural amino acid, p-azido-L-phenylalanine at various targeted positions in GPCRs and show the versatility of the azido group in different applications. These include a targeted photocrosslinking technology to identify residues in the ligand-binding pocket of a GPCR, and site-specific bioorthogonal modification of GPCRs with a peptide-epitope tag or fluorescent...
15.7K
Construction of Model Lipid Membranes Incorporating G-protein Coupled Receptors (GPCRs)09:45

Construction of Model Lipid Membranes Incorporating G-protein Coupled Receptors (GPCRs)

4.0K
This protocol utilizes agarose swelling as a powerful and generalizable technique for incorporating integral membrane proteins (IMPs) into giant unilamellar lipid vesicles (GUVs), as described here for the reconstitution of the human 1A serotonin receptor protein (5-HT1AR), one of the classes of pharmacologically important G protein-coupled...
4.0K
Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

4.0K
G Protein–Coupled Receptors (GPCRs) are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to various stimuli. GPCRs regulate critical physiological pathways and are excellent drug targets for treating diseases such as diabetes, cancer, obesity, depression, or Alzheimer's. Nearly 35% of approved drugs implement their therapeutic effects by selectively interacting with specific GPCRs.
GPCRs are also called heptahelical,...
4.0K

You might also read

Related Articles

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

Sort by
Same author

Biochemical and structural analysis of -AtN-Myc down regulated like-1 reveals phosphatidic acid regulated esterase function.

Plant physiology and biochemistry : PPB·2026
Same author

The interplay between molecular architecture, pharmacology, and suspected adverse drug reactions associated with nonsteroidal androgen antagonists in the United Kingdom.

British journal of clinical pharmacology·2026
Same author

Self-Assembly of Unconventional Triphenylene-Based Frustrated Amphiphile in Solution.

Langmuir : the ACS journal of surfaces and colloids·2026
Same author

An interpretable machine learning framework for adverse drug reaction prediction from drug-target interactions.

PloS one·2026
Same author

Prescribing Patterns and Adverse Effects of Semaglutide: A Real-World Comparative Evaluation.

Healthcare (Basel, Switzerland)·2026
Same author

Triple-action Pt(IV) prodrugs of cisplatin and oxaliplatin with indole propionate and 4-phenylbutyrate ligands as potent anticancer agents.

Journal of inorganic biochemistry·2025
Same journal

The Quantum-to-Classical Transducer: A Thermodynamic and Quantum Mechanical Framework for the Emergence of Bioenergetics.

Bio Systems·2026
Same journal

Forward-backward gene expression binarization for boolean state inference over a known regulatory network.

Bio Systems·2026
Same journal

Partial-Label Metric Ceilings for Evaluating Gene Regulatory Networks Inferred from Single-Cell Foundation Models.

Bio Systems·2026
Same journal

The impedance mismatch theory: A non-equilibrium thermodynamic framework for a shared energetic stress pathway in neurodegeneration.

Bio Systems·2026
Same journal

Immune signal-status misclassification: A theoretical framework for biological status assignment and failed status resolution.

Bio Systems·2026
Same journal

Contextuality, incompatibility, and intra-system entanglement of mental markers: From cognition and decision making to medicine.

Bio Systems·2026
See all related articles

Related Experiment Video

Updated: Jan 20, 2026

Ligand Binding Receptors : G-protein Coupled Receptors
01:21

Ligand Binding Receptors : G-protein Coupled Receptors

131.6K

Information transmission and processing in G-protein-coupled-receptor complexes.

Roger D Jones1, Achille Giacometti2, Alan M Jones3

  • 1Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27514, USA; Dipartimento di Scienze Molecolari e Nanosistemi, Università Ca' Foscari Venezia, 30123 Venezia, Italy; European Centre for Living Technology (ECLT) Ca' Bottacin, 3911 Dorsoduro Calle Crosera, 30123 Venezia, Italy.

Bio Systems
|January 18, 2026
PubMed
Summary
This summary is machine-generated.

We developed a new thermodynamic model for molecular switches like G-protein-coupled receptors (GPCRs). This framework reveals how chemical flux and energy differences control receptor states, offering insights for drug design.

Keywords:
Drug designEntropyG protein-coupled receptor (GPCR)Induced-fit conformationInformation flowNonequilibrium steady statePhosphataseSecond law of thermodynamics

More Related Videos

Quantifying Agonist Activity at G Protein-coupled Receptors
11:45

Quantifying Agonist Activity at G Protein-coupled Receptors

Published on: December 26, 2011

19.8K
G Protein-coupled Receptors
01:15

G Protein-coupled Receptors

16.6K

Related Experiment Videos

Last Updated: Jan 20, 2026

Ligand Binding Receptors : G-protein Coupled Receptors
01:21

Ligand Binding Receptors : G-protein Coupled Receptors

131.6K
Quantifying Agonist Activity at G Protein-coupled Receptors
11:45

Quantifying Agonist Activity at G Protein-coupled Receptors

Published on: December 26, 2011

19.8K
G Protein-coupled Receptors
01:15

G Protein-coupled Receptors

16.6K

Area of Science:

  • Biophysics
  • Molecular Biology
  • Systems Biology

Background:

  • G-protein-coupled receptors (GPCRs) are crucial for cellular signaling but their switching mechanisms are not fully understood.
  • Understanding the physical principles of GPCR state transitions is essential for deciphering cellular information processing.

Purpose of the Study:

  • To develop a general theoretical framework for molecular computation in biological systems.
  • To apply this framework to G-protein-coupled receptors (GPCRs) to elucidate their switching mechanisms.
  • To identify key parameters governing GPCR state transitions using nonequilibrium thermodynamics.

Main Methods:

  • Developed a theoretical model based on nonequilibrium thermodynamics.
  • Identified governing parameters for receptor-state transitions: chemical flux and free-energy differences.
  • Incorporated reciprocal conformation-fit changes between ligand and receptor.

Main Results:

  • Predicted three quasistable GPCR configurations: 'on,' 'off,' and intermediate, optimizing information transmission.
  • Demonstrated that active states sustain chemical flux, while inactive states do not.
  • Showed phosphatase activity determines 'on'/'off' states, while kinase activity maintains flux.

Conclusions:

  • The model provides a generalizable framework for understanding biological switches driven by chemical flux.
  • Predictions align with experimental data, suggesting new drug design targets for GPCRs.
  • The framework extends beyond GPCRs to other biological switching systems.