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

2° Amines to N-Nitrosamines: Reaction with NaNO201:20

2° Amines to N-Nitrosamines: Reaction with NaNO2

4.7K
Secondary amines react with nitrous acid to form N-nitrosamines, as depicted in Figure 1. Nitrous acid, a weak and unstable acid, is formed in situ from an aqueous solution of sodium nitrite and strong acids, such as hydrochloric acid or sulfuric acid, in cold conditions. In the presence of an acid, the nitrous acid gets protonated. The subsequent loss of water results in the formation of the electrophile known as nitrosonium ion.
4.7K
Protein and Protein Structure02:15

Protein and Protein Structure

83.0K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
83.0K
Resonance02:52

Resonance

56.9K
The Lewis structure of a nitrite anion (NO2−) may actually be drawn in two different ways, distinguished by the locations of the N-O and N=O bonds. 
56.9K
Rate-Determining Steps03:08

Rate-Determining Steps

33.8K
Relating Reaction Mechanisms
In a multistep reaction mechanism, one of the elementary steps progresses significantly slower than the others. This slowest step is called the rate-limiting step (or rate-determining step). A reaction cannot proceed faster than its slowest step, and hence, the rate-determining step limits the overall reaction rate.
The concept of rate-determining step can be understood from the analogy of a 4-lane freeway with a short-stretch of traffic-bottleneck caused due to...
33.8K
Resonance and Hybrid Structures02:16

Resonance and Hybrid Structures

21.3K
According to the theory of resonance, if two or more Lewis structures with the same arrangement of atoms can be written for a molecule, ion, or radical, the actual distribution of electrons is an average of that shown by the various Lewis structures.
Resonance Structures and Resonance Hybrids
The Lewis structure of a nitrite anion (NO2−) may actually be drawn in two different ways, distinguished by the locations of the N–O and N=O bonds.
21.3K
Hemoglobin01:24

Hemoglobin

5.5K
Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
5.5K

You might also read

Related Articles

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

Sort by
Same author

Food-Derived Multi-Target Antihypertensive Peptides: Sources, Mechanisms and AI-Driven Strategies.

Foods (Basel, Switzerland)·2026
Same author

Engineering zirconium-based MOFs for selective adsorption of estrogenic contaminants and the application in electrospun solid-phase microextraction.

Journal of hazardous materials·2026
Same author

Effect of a Se-enriched <i>Limosilactobacillus fermentum</i> CGMCC 17434 compound microbial agent synergising with peanut sprouts on the flavor of Se-enriched yogurt.

Food chemistry: X·2026
Same author

Molecular mechanisms of oyster-derived umami peptides: Docking, dynamics simulation, and MM-PBSA analysis based on optimal enzymolysis.

Food chemistry·2026
Same author

Progress in the application of high internal phase emulsions in weight-loss food development: Mechanisms, effects, applications and integration with artificial intelligence.

Food chemistry·2026
Same author

Comparing the impacts of conventional and emerging roasting processes on duck myofibrillar protein structure, volatile profiles, and polycyclic aromatic hydrocarbon formation.

Food research international (Ottawa, Ont.)·2026

Related Experiment Video

Updated: Oct 13, 2025

Chemiluminescence-based Assays for Detection of Nitric Oxide and its Derivatives from Autoxidation and Nitrosated Compounds
08:23

Chemiluminescence-based Assays for Detection of Nitric Oxide and its Derivatives from Autoxidation and Nitrosated Compounds

Published on: February 16, 2022

4.4K

Structural characterization and stability analysis of phosphorylated nitrosohemoglobin.

Xiaoqing Ma1, Yangying Sun1, Daodong Pan1

  • 1State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo 315211, PR China; Key Laboratory of Animal Protein Food Deep Processing Technology of Zhejiang Province, College of Food and Pharmaceutical Sciences, Ningbo University, Ningbo 315800, PR China.

Food Chemistry
|November 12, 2021
PubMed
Summary

Sodium tripolyphosphate (STP) enhances nitrosohemoglobin (NO-Hb) stability through phosphorylation. This modification improves protein resistance to light, oxidants, heat, and pH changes, increasing NO-Hb

Keywords:
C–O–P bondLC-MS/MSPhosphorylation modificationPorcine hemoglobinStability

More Related Videos

Nitropeptide Profiling and Identification Illustrated by Angiotensin II
07:31

Nitropeptide Profiling and Identification Illustrated by Angiotensin II

Published on: June 16, 2019

5.8K
Platelet-based Detection of Nitric Oxide in Blood by Measuring VASP Phosphorylation
07:13

Platelet-based Detection of Nitric Oxide in Blood by Measuring VASP Phosphorylation

Published on: January 7, 2019

8.1K

Related Experiment Videos

Last Updated: Oct 13, 2025

Chemiluminescence-based Assays for Detection of Nitric Oxide and its Derivatives from Autoxidation and Nitrosated Compounds
08:23

Chemiluminescence-based Assays for Detection of Nitric Oxide and its Derivatives from Autoxidation and Nitrosated Compounds

Published on: February 16, 2022

4.4K
Nitropeptide Profiling and Identification Illustrated by Angiotensin II
07:31

Nitropeptide Profiling and Identification Illustrated by Angiotensin II

Published on: June 16, 2019

5.8K
Platelet-based Detection of Nitric Oxide in Blood by Measuring VASP Phosphorylation
07:13

Platelet-based Detection of Nitric Oxide in Blood by Measuring VASP Phosphorylation

Published on: January 7, 2019

8.1K

Area of Science:

  • Biochemistry
  • Protein Chemistry
  • Biophysical Chemistry

Background:

  • Nitrosohemoglobin (NO-Hb) is a modified form of hemoglobin.
  • Understanding protein modifications is crucial for biochemical applications.

Purpose of the Study:

  • To investigate the phosphorylation of NO-Hb using sodium tripolyphosphate (STP).
  • To assess the impact of phosphorylation on NO-Hb structure and stability.

Main Methods:

  • Hydrothermal treatment of NO-Hb with STP.
  • Analysis of protein structure and stability under various conditions (light, oxidant, temperature, pH).
  • Spectrophotometric analysis of NO-Hb and phosphorylated NO-Hb (P-NO-Hb).

Main Results:

  • Phosphate groups bind to NO-Hb via serine and tyrosine residues, forming C-O-P bonds.
  • Hydrothermal treatment with STP maintained α-helix stability, enhancing overall protein stability.
  • Phosphorylated NO-Hb (P-NO-Hb) exhibited significantly increased stability against light, hydrogen peroxide, high temperatures, and non-neutral pH.
  • P-NO-Hb showed nearly double the absorbance of Hb and NO-Hb, with a slower decrease in absorbance over time.

Conclusions:

  • Phosphorylation by STP effectively increases the structural stability of NO-Hb.
  • The observed structural changes, particularly enhanced α-helix stability, contribute to improved protein resilience.
  • Phosphorylated NO-Hb demonstrates superior stability and absorbance properties compared to unmodified NO-Hb.