Amino Acid Hydrolysis
Amino Acid Hydrolysis - Related Videos
04:04
Radiolabeled Amino Acid Uptake Assay to Quantify Cellular Uptake of Amino Acids
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2025
This video demonstrates an in vitro technique for estimating amino acid uptake by bone marrow-derived stromal cells. Na+-dependent amino acid transporters mediate the uptake of radiolabeled amino acids inside the cells, and the cellular uptake is estimated by measuring the radioactivity.
06:44
Hydrolysis of a Ni-Schiff-Base Complex Using Conditions Suitable for Retention of Acid-labile Protecting Groups
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2017
Here, we present an efficient hydrolysis and subsequent Fmoc protection of an amino acid isolated from a Ni-Schiff-base complex. Hydrolysis conditions presented here are suitable for use when retention of acid-labile side-chain protecting groups is required. This technique may be adaptable to a variety of unnatural amino acid substrates.
03:49
Amino acids
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2026
Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible for...
07:26
Metabolic Pathway Confirmation and Discovery Through 13C-labeling of Proteinogenic Amino Acids
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Cited by 53 •
2012
13C-isotope labeling is a useful technique for determining the cell central metabolism for various types of microorganisms. After cells have been cultured with a specific labeled substrate, GC-MS measurement can reveal functional metabolic pathways based on unique labeling patterns in proteinogenic amino acids.
01:08
Hydrolysis of ATP
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2019
The bonds of adenosine triphosphate (ATP) can be broken through the addition of water, releasing one or two phosphate groups in an exergonic process called hydrolysis. This reaction liberates the energy in the bonds for use in the cell—for instance, to synthesize proteins from amino acids. If one phosphate group is removed, a molecule of ADP—adenosine diphosphate—remains, along with inorganic phosphate. ADP can be further hydrolyzed to AMP—adenosine monophosphate—by the removal of a second...
FAQs
Acid or base catalysis promotes cleavage of peptide bonds by water, while heating is often used to support the chemical process. This treatment converts the peptide-linked form of a protein or peptide into a mixture of constituent amino acids, creating a sample suitable for later separation and measurement.
Protease enzymes accelerate peptide-bond cleavage under milder conditions than acid- or base-catalyzed treatment. Their specificity can influence which bonds are cleaved, whereas chemical hydrolysis uses catalytic acid or base and often heating. This distinction matters when researchers need a controlled breakdown process or want to compare products generated under different conditions.
Hydrolysis produces multiple amino acids rather than a single uniform product, so separation is needed before measurement. The measured mixture can reveal the composition of the starting protein or peptide. In biochemistry, this links chemical bond cleavage to practical analysis of protein structure, food and biomaterial quality, and related research questions.
An investigator first subjects a protein or peptide to chemical or enzymatic hydrolysis, selecting acid, base, heating, or a protease-based approach. The resulting amino acid mixture is then separated and measured. Comparing the measured components with the starting material supports compositional analysis rather than merely confirming that peptide-bond cleavage occurred.
By converting proteins in food or biomaterials into measurable constituent amino acids, the method supports assessment of their quality and composition. The hydrolysate provides analytical information that is not available from the intact protein alone. This makes hydrolysis useful when researchers need to characterize protein-containing materials in a biochemical framework.
Breaking proteins and peptides into constituent amino acids connects molecular analysis with nutrient utilization and metabolism, because amino acids are the products examined after cleavage. Hydrolysis also supplies building blocks for biochemical and pharmaceutical research. In protein-structure and peptide-function studies, the resulting composition helps relate molecular materials to their biological or research roles.