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 Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

3.8K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
3.8K
Proteins: Dietary Sources and Requirements01:28

Proteins: Dietary Sources and Requirements

557
Consuming animal-based products offers high-quality proteins that contain optimal levels and combinations of essential amino acids, crucial for tissue repair and growth. Foods like eggs, milk, fish, and most meats are a source of complete proteins. Legumes and cereals are abundant in proteins; however, they typically lack a full range of essential amino acids. As a result, they are considered incomplete protein sources. Some plant sources like soybeans, quinoa, and amaranth do contain complete...
557
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

11.1K
Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
11.1K
Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

3.6K
3.6K
Protein Modifications in the RER01:26

Protein Modifications in the RER

5.4K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
5.4K
Overview of Protein Metabolism01:21

Overview of Protein Metabolism

1.6K
Proteins are broken down into amino acids during digestion. Unlike fats and carbohydrates, which are stored for later use, proteins are not. Instead, amino acids are either used to produce ATP through oxidation or contribute to the creation of new proteins for the growth and repair of the body. Any surplus amino acids from the diet are converted into glucose or triglycerides rather than excreted.
Amino acids play various roles in the body once they are absorbed into cells. They are restructured...
1.6K

You might also read

Related Articles

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

Sort by
Same author

Tasty&Healthy Exclusive Whole-Food Diet in Asymptomatic Children and Young Adults With Biologically Active Crohn's Disease: The TASTI-E Randomized Controlled Trial.

Clinical gastroenterology and hepatology : the official clinical practice journal of the American Gastroenterological Association·2026
Same author

An interventional pilot study protocol on the effect of extra virgin olive oil on women with preeclampsia risk.

Annals of translational medicine·2026
Same author

Bone Turnover Markers (CTX and P1NP) Following Low-Carbohydrate and Mediterranean Diet Interventions in Adolescents and Young Adults with Type 1 Diabetes.

Nutrients·2025
Same author

Antifungal effect and mode of activity of zinc chloride against toxigenic fungus Aspergillus flavus.

Food research international (Ottawa, Ont.)·2025
Same author

Enteral nutrition compared with corticosteroids in children with Crohn's disease: A long-term nationwide study from the epi-IIRN.

Alimentary pharmacology & therapeutics·2024
Same author

Assessment of Relative Energy Deficiency in Sport (REDs) Risk among Adolescent Acrobatic Gymnasts.

Journal of personalized medicine·2024

Related Experiment Video

Updated: Aug 20, 2025

Assays for the Degradation of Misfolded Proteins in Cells
10:56

Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

12.1K

Revisiting Protein Quality Assessment to Include Alternative Proteins.

Efrat Monsonego Ornan1, Ram Reifen1

  • 1Institute of Biochemistry and Nutrition, The Robert H. Smith Faculty of Agriculture, Food and Environment, The Hebrew University of Jerusalem, Rehovot 7610001, Israel.

Foods (Basel, Switzerland)
|November 26, 2022
PubMed
Summary

New preclinical models are needed to assess sustainable protein quality. Postnatal growth showed limitations in conventional protein assessment scores like PDCAAS and DIAAS for alternative protein sources.

Keywords:
amino acidsbone developmentdietlongitudinal growth

More Related Videos

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification
09:04

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Published on: August 17, 2015

17.1K
A Protocol for Functional Assessment of Whole-Protein Saturation Mutagenesis Libraries Utilizing High-Throughput Sequencing
11:36

A Protocol for Functional Assessment of Whole-Protein Saturation Mutagenesis Libraries Utilizing High-Throughput Sequencing

Published on: July 3, 2016

11.0K

Related Experiment Videos

Last Updated: Aug 20, 2025

Assays for the Degradation of Misfolded Proteins in Cells
10:56

Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

12.1K
Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification
09:04

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Published on: August 17, 2015

17.1K
A Protocol for Functional Assessment of Whole-Protein Saturation Mutagenesis Libraries Utilizing High-Throughput Sequencing
11:36

A Protocol for Functional Assessment of Whole-Protein Saturation Mutagenesis Libraries Utilizing High-Throughput Sequencing

Published on: July 3, 2016

11.0K

Area of Science:

  • Nutritional Science
  • Biochemistry
  • Physiology

Background:

  • Growing demand for sustainable protein sources (legumes, insects, algae, cultured meat) necessitates re-evaluating protein quality assessment.
  • Conventional methods like protein digestibility-corrected amino acid score (PDCAAS) and digestible indispensable amino acid score (DIAAS) have limitations for novel and plant-based proteins.

Purpose of the Study:

  • To introduce a sensitive preclinical model for assessing the quality and bioavailability of diverse protein sources.
  • To evaluate the efficacy of conventional protein assessment scores (PDCAAS, DIAAS) against a physiological growth model.

Main Methods:

  • Utilized a preclinical model based on postnatal growth, a key indicator of development and health.
  • Compared growth performance of animals fed various protein sources at adequate and restricted (10% of calories) intake levels.

Main Results:

  • Most alternative proteins performed comparably to casein (animal source) when provided at adequate dietary levels.
  • Under protein restriction, all alternative sources failed to support normal growth.
  • No correlation was observed between growth performance in the preclinical model and PDCAAS/DIAAS values from literature.

Conclusions:

  • The postnatal growth model offers a sensitive approach to evaluate protein quality for diverse sources.
  • Conventional protein assessment scores (PDCAAS, DIAAS) demonstrate significant limitations in reflecting true protein bioavailability and growth impact, especially for alternative proteins.