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

Aldehydes and Ketones with HCN: Cyanohydrin Formation Mechanism01:10

Aldehydes and Ketones with HCN: Cyanohydrin Formation Mechanism

2.9K
Cyanohydrins are formed when cyanide nucleophiles and carbonyl compounds like aldehydes and ketones react. A strong base, the cyanide ion, catalyzes cyanohydrin formation. The ions are generated from HCN under aqueous conditions. Once the cyanide ions are generated, the first step involves the nucleophilic attack of the cyanide ions on the electrophilic carbonyl carbon. This attack shifts the π electrons from the C=O to the oxygen atom forming the alkoxide ion intermediate. The...
2.9K
Aldehydes and Ketones with HCN: Cyanohydrin Formation Overview01:32

Aldehydes and Ketones with HCN: Cyanohydrin Formation Overview

2.5K
Cyanohydrins are compounds that contain –CN and –OH groups on the same carbon atom. They are formed by the nucleophilic addition of the cyanide ions to the carbonyl group. Cyanide ions are highly basic and nucleophilic and can be generated from HCN under aqueous conditions. However, since HCN is a weak acid, the number of cyanide ions generated is very small. Hence, a small amount of base or KCN/NaCN is added to HCN to increase the concentration of the cyanide ions in the reaction...
2.5K
ortho–para-Directing Deactivators: Halogens01:24

ortho–para-Directing Deactivators: Halogens

5.2K
Halogens are ortho–para directors. They are more electronegative than carbon. Therefore, as ring substituents, they can withdraw electrons through the inductive effect and deactivate the aromatic ring towards electrophilic substitution. Halogens also have an electron-donating resonance effect on the ring, which influences the orientation of the incoming electrophile. If an electrophile attacks at the ortho or the para position, the halogen donates electrons and stabilizes the intermediate...
5.2K
Hydrogen Bonds01:04

Hydrogen Bonds

7.7K
A hydrogen bond is formed when a weakly positive hydrogen atom already bonded to one electronegative atom (for example, the oxygen in the water molecule) is attracted to another electronegative atom from another polar molecule, such as water (H2O), hydrogen fluoride (HF), or ammonia (NH3). The huge electronegativity difference between the H atom (2.1) and the atom to which it is bonded (4.0 for an F atom, 3.5 for an O atom, or 3.0 for an N atom), combined with the very small size of an H atom...
7.7K
2D NMR: Overview of Heteronuclear Correlation Techniques01:18

2D NMR: Overview of Heteronuclear Correlation Techniques

108
Heteronuclear correlation spectroscopy is an analytical technique that investigates the coupling between different types of nuclei, often a proton and an X-nucleus, such as carbon-13 or nitrogen-15. This method is commonly used in nuclear magnetic resonance (NMR) spectroscopy to gain insights into complex chemical compounds' structural and compositional aspects. A typical heteronuclear correlation spectrum displays X-nucleus chemical shifts on one axis and a proton spectrum on the other...
108
2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)01:19

2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)

581
Heteronuclear single-quantum correlation spectroscopy (HSQC) is a 2D NMR technique that reveals one-bond correlations between hydrogen and a heteronucleus. The HSQC experiment is similar to the heteronuclear correlation experiment (HETCOR) but is more sensitive. In the HSQC spectrum, the proton chemical shift is plotted on the horizontal F2 axis, while the 13C chemical shift is plotted on the vertical F1 axis. The corresponding proton and 13C spectra are also shown. The HSQC contour plot does...
581

You might also read

Related Articles

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

Sort by
Same author

K channels and action potential in dorsal root ganglion of diverse animals.

Comparative biochemistry and physiology. Toxicology & pharmacology : CBP·2025
Same author

Delineation and functions of HCN channels in neurons.

Progress in biophysics and molecular biology·2025
Same author

Off-Target hERG Blockade by Ivabradine.

JACC. Clinical electrophysiology·2025
Same author

Comparison of Superoxide Dismutase Activity at the Cell, Organ, and Whole-Body Levels.

Cell biochemistry and biophysics·2025
Same author

Long-term spontaneous membrane currents in DRG neurons.

Journal of receptor and signal transduction research·2025
Same author

Deciphering the peculiarities of cell types in the septum.

Neuroscience·2024

Related Experiment Video

Updated: May 13, 2025

Method for Identifying Small Molecule Inhibitors of the Protein-protein Interaction Between HCN1 and TRIP8b
10:20

Method for Identifying Small Molecule Inhibitors of the Protein-protein Interaction Between HCN1 and TRIP8b

Published on: November 11, 2016

8.5K

Roles of funny HCN.

Sodikdjon A Kodirov1

  • 1Pavlov Institute of Physiology, Russian Academy of Sciences, Saint Petersburg, Russia; Institute of Physiology and Pathophysiology, University of Mainz, Germany; University of Texas at Brownsville, Department of Biological Sciences, TX 78520, USA; Instituto de Medicina Molecular, Universidade de Lisboa, Lisbon, Portugal; Institute of Biophysics, Johannes Kepler University, Linz, Austria.

Comparative Biochemistry and Physiology. Toxicology & Pharmacology : CBP
|April 15, 2025
PubMed
Summary

Hyperpolarization-activated cyclic nucleotide-gated (HCN) channels, crucial for heart rhythm, share similarities with potassium channels and interact with VAMP proteins. This interaction influences channel function and may link HCN channels to various pathologies.

Keywords:
HCNI(f) currentKv2LQTPatch-clampSagSynaptobrevinVAMP

More Related Videos

Infrared Degenerate Four-wave Mixing with Upconversion Detection for Quantitative Gas Sensing
10:42

Infrared Degenerate Four-wave Mixing with Upconversion Detection for Quantitative Gas Sensing

Published on: March 22, 2019

6.2K
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

12.2K

Related Experiment Videos

Last Updated: May 13, 2025

Method for Identifying Small Molecule Inhibitors of the Protein-protein Interaction Between HCN1 and TRIP8b
10:20

Method for Identifying Small Molecule Inhibitors of the Protein-protein Interaction Between HCN1 and TRIP8b

Published on: November 11, 2016

8.5K
Infrared Degenerate Four-wave Mixing with Upconversion Detection for Quantitative Gas Sensing
10:42

Infrared Degenerate Four-wave Mixing with Upconversion Detection for Quantitative Gas Sensing

Published on: March 22, 2019

6.2K
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

12.2K

Area of Science:

  • Neuroscience
  • Cardiology
  • Molecular Biology

Background:

  • Hyperpolarization-activated cyclic nucleotide-gated (HCN) channels are primarily known for their role in pacemaking.
  • Recent studies suggest HCN channels are implicated in arrhythmias and seizures, conditions often linked to voltage-dependent K+ (Kv) and Na+ (Nav) channels, and neurotransmitters.
  • HCN channels exhibit functional parallels with Kv channels, including links to long QT interval and potential roles in epilepsy and other brain pathologies.

Purpose of the Study:

  • To explore the functional similarities and interactions of HCN channels with other ion channels and proteins.
  • To investigate the newly discovered interaction between HCN channels and vesicle-associated membrane proteins (VAMP).
  • To understand the implications of these interactions for channel function and associated diseases.

Main Methods:

  • Comparative analysis of HCN and Kv channel properties.
  • Investigation of HCN channel interactions with VAMP proteins, specifically VAMP-associated protein B (VAPB).
  • Examination of the effect of HCN antagonists on Kv channels, such as HERG (Kv11.1).

Main Results:

  • HCN channels share functional similarities with Kv channels, including involvement in long QT interval and potential links to arrhythmias and epilepsy.
  • A novel interaction between HCN channels and VAMP proteins, particularly VAPB, has been identified.
  • The drug ivabradine, a selective HCN channel antagonist, also inhibits IKr current through HERG (Kv11.1) channels, highlighting a significant functional overlap.

Conclusions:

  • HCN channels, while distinct, share crucial functional similarities and interactions with Kv channels.
  • The interaction with VAMP proteins represents a novel regulatory mechanism for HCN channel function.
  • Pharmacological agents targeting HCN channels may have off-target effects on Kv channels, suggesting complex therapeutic implications.