Polar amino acids possess side chains capable of interacting with water owing to the presence of electronegative elements like oxygen, nitrogen, or sulfur.
Amino acids are building blocks of proteins, and the only way to get them is to eat protein. We can classify the amino acids found in proteins as either "essential" or "non-essential" for your health.
Three of the most important necessary amino acids are leucine, isoleucine, and valine, which are the components that make up branched-chain amino acids (BCAAs).
Amino acids can be divided into polar and nonpolar groups according to the polarity of the side chains by using this classification system.
The characteristics of the side chains of amino acids are used to categorize them. These side chains are responsible for determining the amino acids' solubility, interactions, and positions within protein structures.
Alanine (Ala) is an amino acid frequently present in proteins. It is categorized as a non-essential amino acid as the human body can produce it from pyruvate, a byproduct of glucose metabolism.
L-Arginine (L-Arg) is an essential amino acid that plays a role in cellular development, ammonia detoxification, and the creation of creatine.
The non-essential amino acid asparagine (Asn) has a role in the metabolic regulation of cellular activities in brain and nerve tissue.
Aspartic acid (aspartate, Asp) is a biologically non-essential amino acid identified by the hydrolysis of asparagine.
Cysteine is a naturally occurring amino acid present in limited amounts in the majority of proteins. It is the sole amino acid that possesses a thiol in its side chain.
Glutamic acid (Glutamate) is a nonessential amino acid mostly utilized and synthesized as its sodium salt, monosodium glutamate (MSG).
Glutamine is the predominant amino acid in plasma, and its significance for good cellular growth in culture has been recognized since the 1950s.
Glycine is the smallest of the amino acids and con-sists of a carbon molecule attached to an amino and a carboxyl group.
Histidine (His) is an important amino acid that has a specific role in the histaminergic system, erythropoiesis, proton buffering, metal ion chelation, and reactive oxygen and nitrogen species scavenging.
Since the body is unable to produce isoleucine on its own, this amino acid must be consumed in the form of food.
In animal nutrition, leucine (Leu) is a crucial branched-chain amino acid (BCAA). In meals that are rich in protein, it is often one of the most abundant amino acids.
Lysine cannot be produced by the majority of higher organisms and is hence an essential amino acid (IAA) that must be ingested in sufficient quantities to support protein synthesis.
The amino acid methionine, or Met, is essential for human nutrition. It plays an important role in metabolism and the synthesis of proteins.
Phenylalanine (Phe) is an important amino acid that possesses both glucogenic and ketogenic properties and is metabolized to tyrosine by phenylalanine hydroxylase.
Proline and its metabolite, hydroxyproline, are distinctive amino acids both chemically and biochemically. They represent one-third of amino acids in collagen proteins, which account for around 30% of body proteins.
In 1865, the German chemist Emil Cramer recognized l-serine (Ser) in silk protein for the first time. It is one of the most common amino acids present in vertebrate proteins.
Threonine (Thr), also known as α-amino-β-hydroxybutyric acid, is a glucogenic and ketogenic necessary amino acid. Human plasma levels of threonine can be significantly raised by supplementation.
Tryptophan, often known as Trp, is an essential amino acid that contains indole and is required for both appropriate child development and growth as well as for adults to maintain nitrogen balance.
Living systems rely on L-tyrosine (Tyr), also known as tyrosine or 4-hydroxyphenylalanine, one of the twenty standard amino acids and one of the non-essential ones utilized by cells in protein synthesis.
Valine (Val) is an essential amino acid and a type of branched-chain amino acid. Due to the involvement of branched-chain amino acids in various metabolic pathways, there has been a surge of interests in valine nutrition and its role in animal physiology.
Amino acids are carbon, hydrogen, oxygen, nitrogen, and sulphur atoms organic molecules. They’re the structural units of proteins, and of many major molecules in life.
Amino acids are the building blocks of life, forming the structural and functional basis of proteins, enzymes and other biomolecules.
Amino acid therapy is a therapy which restores and enhances the body’s neurotransmitter system by replenishing with amino acids.
L-amino acids and D-amino acids are stereoisomers of amino acids, which have their own roles in nature, but are related to one another.
The peptides have become very interesting because of their distinct biological role and huge applicability potential.
