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

Phosphorylation01:02

Phosphorylation

53.7K
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
53.7K
What is Conservation Biology?01:57

What is Conservation Biology?

24.0K
Conservation biology is a scientific field that focuses on the preservation of biodiversity in order to protect ecosystems while meeting the needs of the human population. Humans require properly functioning ecosystems to maintain our supply of natural resources, including food, medicines, and building materials.
24.0K
Biological Effects of Radiation02:59

Biological Effects of Radiation

17.7K
All radioactive nuclides emit high-energy particles or electromagnetic waves. When this radiation encounters living cells, it can cause heating, break chemical bonds, or ionize molecules. The most serious biological damage results when these radioactive emissions fragment or ionize molecules. For example, α and β particles emitted from nuclear decay reactions possess much higher energies than ordinary chemical bond energies. When these particles strike and penetrate matter, they...
17.7K
Second Order systems II01:18

Second Order systems II

396
In an underdamped second-order system, where the damping ratio ζ is between 0 and 1, a unit-step input results in a transfer function that, when transformed using the inverse Laplace method, reveals the output response. The output exhibits a damped sinusoidal oscillation, and the difference between the input and output is termed the error signal. This error signal also demonstrates damped oscillatory behavior. Eventually, as the system reaches a steady state, the error diminishes to zero.
396
First Order Systems01:21

First Order Systems

412
First-order systems, such as RC circuits, are foundational in understanding dynamic systems due to their straightforward input-output relationship. Analyzing their responses to different input functions under zero initial conditions reveals significant insights into system behavior.
When a first-order system is subjected to a unit-step input, its response is characterized by its transfer function. By applying the Laplace transform of the unit-step input to the transfer function, expanding the...
412
Second Order systems I01:20

Second Order systems I

581
A servo system exemplifies a second-order system, featuring a proportional controller and load elements that ensure the output position aligns with the input position. The relationship between these components is described by a second-order differential equation. Applying the Laplace transform under zero initial conditions yields the transfer function, showing how inputs are converted to outputs in the system.
By reinterpreting the system, one can derive the closed-loop transfer function, which...
581

You might also read

Related Articles

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

Sort by
Same author

Protease mimicry: Dissecting the ester bond crosslinking mechanics in bacterial adhesin proteins.

Protein science : a publication of the Protein Society·2025
Same author

Feedback regulation of iron-sulfur cluster biogenesis.

bioRxiv : the preprint server for biology·2025
Same author

Structures of Mycobacterium tuberculosis isoprenyl diphosphate synthase Rv2173 in substrate-bound forms.

Acta crystallographica. Section F, Structural biology communications·2025
Same author

Evidence of a Catalytic Dyad in F<sub>420</sub>-Dependent Glucose-6-phosphate Dehydrogenase from <i>Mycobacterium tuberculosis</i>.

Biochemistry·2024
Same author

Poetry in motion: catching molecules in action.

IUCrJ·2024
Same author

Poly-γ-glutamylation of biomolecules.

Nature communications·2024

Related Experiment Video

Updated: Jan 25, 2026

Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay
09:17

Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay

Published on: January 11, 2017

9.0K

Histidine phosphorylation in biological systems.

Jennifer Puttick1, Edward N Baker, Louis T J Delbaere

  • 1Department of Biochemistry, University of Saskatchewan, Saskatoon, Saskatchewan, Canada.

Biochimica Et Biophysica Acta
|August 31, 2007
PubMed
Summary

Phosphohistidine residues, though crucial in biological processes, are unstable. Stable forms in proteins are often stabilized by ion-pair hydrogen bonds, revealing insights into their function.

More Related Videos

The Use of Chemostats in Microbial Systems Biology
13:19

The Use of Chemostats in Microbial Systems Biology

Published on: October 14, 2013

31.7K
Synthesis and Calibration of Phosphorescent Nanoprobes for Oxygen Imaging in Biological Systems
10:38

Synthesis and Calibration of Phosphorescent Nanoprobes for Oxygen Imaging in Biological Systems

Published on: March 3, 2010

14.3K

Related Experiment Videos

Last Updated: Jan 25, 2026

Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay
09:17

Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay

Published on: January 11, 2017

9.0K
The Use of Chemostats in Microbial Systems Biology
13:19

The Use of Chemostats in Microbial Systems Biology

Published on: October 14, 2013

31.7K
Synthesis and Calibration of Phosphorescent Nanoprobes for Oxygen Imaging in Biological Systems
10:38

Synthesis and Calibration of Phosphorescent Nanoprobes for Oxygen Imaging in Biological Systems

Published on: March 3, 2010

14.3K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Histidine phosphorylation is a significant post-translational modification in prokaryotes and occurs in eukaryotes.
  • Phosphohistidine residues are generally unstable due to rapid hydrolysis, limiting their observation in proteins.
  • Key biological processes like the phosphoenolpyruvate:sugar phosphotransferase system (PTS) and bacterial two-component systems utilize phosphohistidines.

Purpose of the Study:

  • To investigate the structural basis for the stability of phosphohistidine residues in proteins.
  • To understand the common features of stable phosphohistidine-containing proteins.

Main Methods:

  • Analysis of existing crystal structures of phosphohistidine-containing proteins.
  • Identification of conserved structural motifs and interactions.

Main Results:

  • While NMR structures of phosphohistidine moieties exist, X-ray structures of PTS proteins are lacking.
  • Crystal structures of nucleoside diphosphate kinase, succinyl-CoA synthetase, cofactor-dependent phosphoglycerate mutase, and protein PAE2307 reveal stable phosphohistidines.
  • A recurring feature in stable phosphohistidines is the presence of ion-pair hydrogen bonds (salt bridges).

Conclusions:

  • Stable phosphohistidines are often stabilized by interactions with acidic amino acid side chains.
  • These ion-pair hydrogen bonds involve the non-phosphorylated nitrogen of the histidine imidazole ring.
  • Understanding these stabilizing interactions is key to studying phosphohistidine function in various biological systems.