Biochemistry of Amino Acids and Hormones

<p>Supporting growth in infants (B)</p> Signup and view all the answers

<p>Most amino acids are optically active except glycine (D)</p> Signup and view all the answers

<p>Amphoteric properties (B)</p> Signup and view all the answers

<p>γ-Carboxyglutamate (A)</p> Signup and view all the answers

<p>Contributing to the ammonia removal process (B)</p> Signup and view all the answers

<p>Increases blood glucose levels (A)</p> Signup and view all the answers

<p>It initiates the contractions of the uterus (A)</p> Signup and view all the answers

<p>It decreases glomerular filtration rate (GFR) (B)</p> Signup and view all the answers

<p>Promotes secretion of steroid hormones from the adrenal cortex (B)</p> Signup and view all the answers

<p>9 amino acids (B)</p> Signup and view all the answers

<p>It acts as a biological antioxidant. (B)</p> Signup and view all the answers

<p>Promotes diuresis and decreases blood pressure (A)</p> Signup and view all the answers

<p>TRH (thyrotropin releasing hormone) (D)</p> Signup and view all the answers

<p>Proteins contain more than 50 amino acids. (D)</p> Signup and view all the answers

<p>Primary structure (A)</p> Signup and view all the answers

<p>Hydrogen bonds (D)</p> Signup and view all the answers

<p>Quaternary structure (A)</p> Signup and view all the answers

<p>Linear sequence of amino acids (C)</p> Signup and view all the answers

<p>The end with a free amine group (C)</p> Signup and view all the answers

<p>Twisting of the polypeptide backbone (D)</p> Signup and view all the answers

<p>The protein may lose its functionality. (C)</p> Signup and view all the answers

<p>Proline (A)</p> Signup and view all the answers

<p>Positively charged (-NH3+) (A)</p> Signup and view all the answers

<p>Physical classification (B)</p> Signup and view all the answers

<p>Nonpolar hydrophobic amino acids (B)</p> Signup and view all the answers

<p>Enantiomers (D)</p> Signup and view all the answers

<p>They can be converted into glucose. (D)</p> Signup and view all the answers

<p>Polar hydrophilic uncharged amino acids (D)</p> Signup and view all the answers

<p>Leucine (D)</p> Signup and view all the answers

<p>Aspartate (B)</p> Signup and view all the answers

<p>Lysine and Leucine (A)</p> Signup and view all the answers

<p>Histidine (B)</p> Signup and view all the answers

<p>GABA (D)</p> Signup and view all the answers

<p>Phenylalanine and Tyrosine (A)</p> Signup and view all the answers

<p>Arginine and Ornithine (D)</p> Signup and view all the answers

<p>Monoiodotyrosine (C)</p> Signup and view all the answers

<p>Serine and Glycine (C)</p> Signup and view all the answers

<p>Glutathione (D)</p> Signup and view all the answers

<p>It acts as a vasodilator and mediates pain sensation. (A)</p> Signup and view all the answers

<p>To provide natural pain relief and enhance mood. (B)</p> Signup and view all the answers

<p>10 (A)</p> Signup and view all the answers

<p>It is a dipeptide synthesized from phenylalanine and L-aspartic acid. (B)</p> Signup and view all the answers

<p>It prevents oxidation of sulfhydryl groups in proteins. (B)</p> Signup and view all the answers

<p>Met-enkephalin (A)</p> Signup and view all the answers

<p>Hemolytic anemia. (B)</p> Signup and view all the answers

They are a group of 20 organic molecules that serve as the building blocks of proteins. These molecules contain a central carbon atom bonded to an amino group (NH2), a carboxyl group (COOH), a hydrogen atom (H), and a side chain (R) which determines the amino acid's unique properties

In proteins, they are always alpha-amino acids, which means the amino group is attached to the carbon atom next to the carboxyl group.

Amino acids exist in two forms: D and L, which are mirror images of each other. Proteins use only L-form amino acids.

The side chain (R) can vary, giving each amino acid unique properties like polarity, charge, size, and shape. These properties affect how the amino acid interacts with other molecules and helps determine the protein's structure and function.

Amino acids are classified based on their side chain's polarity. Based on how they interact with water: Nonpolar, Polar uncharged and Polar Charged

Nonpolar amino acids have hydrophobic side chains, meaning they don't interact well with water and prefer to be grouped together. They are important for protein folding, stability, and membrane interactions.

Polar uncharged amino acids have side chains that interact with water through hydrogen bonds. They contribute to protein solubility and stability, and are often found on the protein surface.

Polar charged amino acids have side chains with a net positive or negative charge. They play crucial roles in protein function, such as enzyme activity, DNA binding, and ion transport.

Amino acids with a hydroxyl group (-OH) attached to their side chain, such as serine, threonine, tyrosine, hydroxylysine, and hydroxyproline.

These amino acids contain an amide group (-CONH2) in their side chain, examples are glutamine and asparagine.

These amino acids carry a positive charge on their side chain (R group) due to the presence of basic groups like lysine, arginine, and histidine.

These amino acids carry a negative charge on their side chain (R group) due to the presence of acidic groups like aspartate and glutamate.

Amino acids that the body cannot synthesize and must be obtained from the diet, these are essential for proper growth, health, and protein synthesis.

Amino acids that can be synthesized by the body but not in sufficient amounts, especially in children.

These amino acids are synthesized in the body in sufficient amounts for both children and adults. These include the remaining amino acids not classified as essential or semiessential.

Amino acids that are not directly incorporated into proteins, but play crucial roles in various metabolic processes.

A dipeptide formed by the joining of two cysteine molecules. It is crucial for maintaining the structure of proteins.

A modified amino acid found in collagen and gelatin. It is formed by the addition of a hydroxyl group to proline.

A modified amino acid found in collagen and gelatin. It is formed by the addition of a hydroxyl group to lysine.

A modified amino acid found in muscle protein myosin. It is formed by the addition of a methyl group to lysine.

A modified amino acid found in muscle protein myosin. It is formed by the addition of a methyl group to histidine.

A modified amino acid found in prothrombin and bone protein. It is formed by the addition of a carboxyl group to glutamate.

A complex amino acid found in elastin, formed by the linking of four lysine residues. It provides elasticity to tissues.

Amino acids are essential for growth and development. They provide building blocks for proteins, hormones, and enzymes.

A hormone produced by the beta cells of the pancreas, responsible for lowering blood glucose levels. It consists of 30 amino acids followed by 21 amino acids.

A hormone produced by the alpha cells of the pancreas, responsible for increasing blood glucose levels. It consists of 29 amino acids.

A hormone secreted by the posterior pituitary gland. It consists of 9 amino acids and stimulates uterine contractions. It plays a crucial role in childbirth by initiating and completing labor.

A hormone secreted by the posterior pituitary gland. It is also called antidiuretic hormone (ADH) and consists of 9 amino acids. It helps regulate water balance in the body by decreasing glomerular filtration rate (GFR) and retaining water.

A peptide consisting of 28 amino acids produced by specialized cells in the heart and nervous tissue. It acts to counteract the effects of vasopressin by promoting the production of dilute urine and lowering blood pressure.

A hormone produced by the anterior pituitary gland that stimulates the adrenal cortex to secrete steroid hormones. It consists of 39 amino acids.

A hormone produced by the anterior pituitary gland that stimulates the release of thyrotropin (TSH) from the anterior pituitary. It consists of 3 amino acids.

A tripeptide consisting of glutamic acid, cysteine, and glycine. Found in all mammalian cells except neurons, it plays important roles as an antioxidant and in amino acid absorption.

A linear sequence of amino acids (AAs) linked by peptide bonds forming a backbone. This structure is determined by the genetic information in DNA, dictating the order of AAs.

The spatial arrangement of amino acids close to each other in the polypeptide chain. This structure arises from interactions between adjacent amino acid residues, like hydrogen bonding.

The overall 3-dimensional structure of a protein, formed by the folding and interactions of the polypeptide chain. This structure is critical for protein function.

The arrangement of multiple polypeptide chains (subunits) within a protein complex. This structure is only present in proteins made up of more than one polypeptide chain.

The covalent bond that links amino acids together in a polypeptide chain. It is a strong bond that gives the protein its backbone.

A type of secondary structure where the polypeptide chain coils into a helix shape. This structure is stabilized by hydrogen bonds between amino acids.

A type of secondary structure where the polypeptide chain folds into a sheet-like structure with hydrogen bonds between adjacent strands.

Any change in the 3-dimensional structure of a protein. This can affect the protein's function and may lead to disease.

Glutathione (GSH) is a tripeptide, a molecule composed of three amino acids: cysteine, glycine, and glutamate. It's a crucial antioxidant found in most cells. It plays a vital role in protecting cells from oxidative damage caused by free radicals, detoxifying harmful substances, and even boosting the immune system.

Glutathione is a powerful antioxidant that scavenges free radicals and peroxides, preventing them from causing damage to cells. This action safeguards tissues and organs from oxidative stress.

By combining with toxic compounds, glutathione helps neutralize them, making them less harmful to the body. This detoxification process aids in protecting the body from harmful chemicals and toxins.

Bradykinin is a potent vasodilator, causing blood vessels to widen and lowering blood pressure. It also causes smooth muscles to contract, aiding in various bodily functions.

Enkephalins are pentapeptide neurotransmitters produced by the brain. They act as natural pain relievers by binding to specific receptors in the brain.

Aspartame is a dipeptide, a compound made of two amino acids: phenylalanine and aspartic acid. It's a popular artificial sweetener known for its intensely sweet taste.

Beta-endorphin is a peptide hormone released by the pituitary gland and hypothalamus. It acts as a powerful pain reliever, similar to morphine, and has a significant impact on mood and emotions, contributing to feelings of pleasure.

Valinomycin is an antibiotic that acts by interfering with the function of certain cellular processes. Bleomycin is an antitumor agent that disrupts DNA replication in cancer cells.