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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

14.7K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Protein and Protein Structure02:15

Protein and Protein Structure

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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...
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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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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...
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What are Proteins?01:55

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Overview
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Protein Networks02:26

Protein Networks

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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
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Protein Families02:47

Protein Families

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Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key...
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Related Experiment Video

Updated: Feb 7, 2026

Green Fluorescent Protein-based Expression Screening of Membrane Proteins in Escherichia coli
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Green Fluorescent Protein-based Expression Screening of Membrane Proteins in Escherichia coli

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Protein.

Malcolm Watford1, Guoyao Wu2

  • 1Department of Nutritional Sciences, Rutgers University, New Brunswick, NJ.

Advances in Nutrition (Bethesda, Md.)
|July 31, 2018
PubMed
Summary

Dietary protein quality depends on the 9 essential amino acids that adults cannot synthesize. Understanding amino acid metabolism is crucial for nutritional science and health.

Area of Science:

  • Nutritional Biochemistry
  • Human Physiology

Background:

  • Proteins are amino acid polymers crucial for bodily functions.
  • Nutritional focus is on the primary amino acid sequence and 20 canonical amino acids, plus 5 others with significant roles.
  • Amino acid metabolism is primarily linked to protein turnover, with nitrogen excreted as urea and ammonia.

Purpose of the Study:

  • To define the nutritional importance of amino acids.
  • To differentiate between indispensable, dispensable, and conditionally indispensable amino acids.
  • To highlight the significance of dietary protein quality, specifically the ratio of essential amino acids.

Main Methods:

  • Analysis of amino acid synthesis pathways in adult humans.
  • Identification of nutritionally indispensable amino acids based on the body's inability to synthesize their carbon skeletons.

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  • Review of amino acid utilization for protein resynthesis and non-protein product synthesis.

    • Main Results:

    • Nine amino acids (leucine, valine, isoleucine, histidine, lysine, methionine, threonine, tryptophan, phenylalanine) are nutritionally indispensable for adults.
    • Cysteine and tyrosine are synthesized from indispensable precursors methionine and phenylalanine, respectively.
    • Most other amino acids can be synthesized from glucose, but some (glutamine, glutamate, glycine, proline, arginine) can become conditionally indispensable.

    Conclusions:

    • Dietary protein assessment requires consideration of both quantity and quality (essential amino acid profile).
    • The body's capacity to synthesize amino acids dictates nutritional requirements.
    • Understanding amino acid metabolism is fundamental to human nutrition and health.