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

Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
Protein Transport to the Stroma01:24

Protein Transport to the Stroma

Chloroplasts are triple membrane structures with an outer membrane, an inner membrane, and a thylakoid membrane, each containing distinct metabolite transporters, membrane translocons, and enzymes. Appropriate sorting and translocating these proteins to their correct membrane systems is essential for chloroplast function.
Protein complexes called the translocon of the outer chloroplast membrane or TOC complex, and the translocon of the inner chloroplast membrane or TIC complex mediate the...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...

You might also read

Related Articles

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

Sort by
Same author

Chassis Selection and Metabolic Fine-Tuning Enable Efficient in planta Betalain Production.

Plant physiology·2026
Same author

Environmental stress reveals new insights regarding proteome rebalancing in Arabidopsis thaliana seeds.

The Plant journal : for cell and molecular biology·2026
Same author

Designing a nitrogen-efficient cold-tolerant maize for modern agricultural systems.

The Plant cell·2025
Same author

Grass Rhizome Proteomics Reveals Convergent Freezing-Tolerance Strategies.

bioRxiv : the preprint server for biology·2025
Same author

Multiple methods for assessing learning and memory in <i>Drosophila melanogaster</i> demonstrates the highly complex, context-dependent genetic underpinnings of cognitive traits.

bioRxiv : the preprint server for biology·2025
Same author

Amino Acid Quantification from Maize Tissues.

Cold Spring Harbor protocols·2024
Same journal

Emerging Trends in Mass Spectrometry-Based Quantitative Proteome and Phosphoproteome Profiling in Maize.

Cold Spring Harbor protocols·2026
Same journal

Sample Preparation for Quantitative Proteome and Phosphoproteome Profiling of Maize Tissues.

Cold Spring Harbor protocols·2026
Same journal

High-Throughput Microbial Assay for Amino Acid Measurement in Ground Maize Seed Samples Utilizing Auxotrophic <i>E. coli</i>.

Cold Spring Harbor protocols·2025
Same journal

Grain Quality in Maize.

Cold Spring Harbor protocols·2025
Same journal

High-Throughput Assay for Measuring Phytate and Available Phosphorus in Ground Maize Seed Samples.

Cold Spring Harbor protocols·2025
Same journal

Functional Genomic Analysis of Transposon Insertion Mutant Maize Plants from the UniformMu National Public Resource.

Cold Spring Harbor protocols·2025
See all related articles

Related Experiment Video

Updated: May 11, 2026

Quantification of Fungal Colonization, Sporogenesis, and Production of Mycotoxins Using Kernel Bioassays
10:01

Quantification of Fungal Colonization, Sporogenesis, and Production of Mycotoxins Using Kernel Bioassays

Published on: April 23, 2012

18.1K

High-Throughput Protein-Bound Amino Acid Quantification from Maize Kernels.

Huda Ansaf1, Abou Yobi1, Ruthie Angelovici2

  • 1Christopher S. Bond Life Sciences Center, Division of Biological Sciences, Interdisciplinary Plant Group, University of Missouri, Columbia, Missouri 65211, USA.

Cold Spring Harbor Protocols
|December 23, 2024
PubMed
Summary
This summary is machine-generated.

Improving maize seed quality requires accurate amino acid quantification. This study presents a high-throughput method to measure all 20 protein-forming amino acids in crude protein extracts, aiding nutritional improvement efforts.

More Related Videos

High-throughput, Microscale Protocol for the Analysis of Processing Parameters and Nutritional Qualities in Maize Zea mays L.
05:55

High-throughput, Microscale Protocol for the Analysis of Processing Parameters and Nutritional Qualities in Maize Zea mays L.

Published on: June 16, 2018

6.9K
Quantifying Plant Soluble Protein and Digestible Carbohydrate Content, Using Corn Zea mays As an Exemplar
07:19

Quantifying Plant Soluble Protein and Digestible Carbohydrate Content, Using Corn Zea mays As an Exemplar

Published on: August 6, 2018

19.8K

Related Experiment Videos

Last Updated: May 11, 2026

Quantification of Fungal Colonization, Sporogenesis, and Production of Mycotoxins Using Kernel Bioassays
10:01

Quantification of Fungal Colonization, Sporogenesis, and Production of Mycotoxins Using Kernel Bioassays

Published on: April 23, 2012

18.1K
High-throughput, Microscale Protocol for the Analysis of Processing Parameters and Nutritional Qualities in Maize Zea mays L.
05:55

High-throughput, Microscale Protocol for the Analysis of Processing Parameters and Nutritional Qualities in Maize Zea mays L.

Published on: June 16, 2018

6.9K
Quantifying Plant Soluble Protein and Digestible Carbohydrate Content, Using Corn Zea mays As an Exemplar
07:19

Quantifying Plant Soluble Protein and Digestible Carbohydrate Content, Using Corn Zea mays As an Exemplar

Published on: August 6, 2018

19.8K

Area of Science:

  • Agricultural Science
  • Biochemistry
  • Analytical Chemistry

Background:

  • Seed quality in crops like maize is significantly influenced by protein-bound amino acid composition.
  • Maize seeds are deficient in essential amino acids lysine and tryptophan due to zein protein dominance.
  • Improving maize nutritional value is crucial, but limited high-throughput quantification methods hinder progress.

Purpose of the Study:

  • To develop and describe a robust, efficient, and high-throughput method for quantifying all 20 proteogenic amino acids from crude protein extracts.
  • To overcome the limitations of existing methods for large-scale population screening in maize.

Main Methods:

  • Protein hydrolysis to release amino acids from the protein backbone.
  • Aqueous extraction of the liberated amino acids.
  • Ultra-performance liquid chromatography-tandem mass spectrometry (UPLC-MS/MS) with multiple reaction monitoring (MRM) for separation, detection, and quantification.
  • Data analysis using MassLynx and TargetLynx software.

Main Results:

  • Successful quantification of all 20 proteogenic amino acids from crude protein extracts.
  • The described method is robust, efficient, and suitable for high-throughput applications.
  • Enables precise measurement of amino acid profiles crucial for seed nutritional quality.

Conclusions:

  • This protocol provides a valuable tool for advancing research in cereal crop nutritional improvement.
  • Facilitates the screening of large populations for enhanced amino acid content, particularly lysine and tryptophan in maize.
  • Supports efforts to develop more nutritious food and feed sources.