Essential and Nonessential Amino Acids Quiz

These amino acids contain a straight chain of carbon atoms with no ring structures. Examples include glycine, alanine, serine, and valine.

They include glycine, alanine, serine, threonine, cysteine, cystine, methionine, valine, leucine and isoleucine.

These amino acids have a carboxyl group (COOH) as part of their side chain, making them acidic.

These amino acids have an amino group (NH2) as part of their side chain, making them basic.

These amino acids have a benzene ring as part of their side chain. Examples include phenylalanine, tyrosine, and tryptophan.

These amino acids are essential to be taken in diet. They are important for growth, health and protein synthesis.

These amino acids are formed in the body in amount enough for adults, but not for growing children.

These amino acids can be synthesized by the body. They do not need to be obtained from the diet.

The linear sequence of amino acids in a protein chain, determined by the DNA sequence.

The three-dimensional structure of a protein, including its overall shape and folding patterns.

The type of bond that holds amino acids together in a polypeptide chain, formed by the reaction between the carboxyl group of one amino acid and the amino group of another.

The arrangement of the polypeptide backbone into repeating structures, such as alpha-helices and beta-sheets.

A spiral structure formed by the coiling of the polypeptide chain, stabilized by hydrogen bonds.

A sheet-like structure formed by the alignment of polypeptide chains, stabilized by hydrogen bonds between adjacent strands.

The final three-dimensional structure of a protein, resulting from interactions between side chains and the polypeptide backbone, determining its function.

The arrangement of multiple polypeptide chains (subunits) into a functional protein complex.

Leucine is the only amino acid that can be broken down directly into ketone bodies, bypassing the process of glucose production. It is not used to make glucose.

These amino acids can be used to generate both glucose and ketone bodies, providing flexibility in energy production.

Amino acids, except glycine, have an asymmetric alpha-carbon. This creates two mirror-image forms known as D and L isomers.

Glycine has two hydrogen atoms attached to its alpha-carbon, making it symmetrical and lacking optical activity. It's the only amino acid without this property.

Amino acids contain both a carboxyl group (-COOH) and an amino group (-NH3+) which makes them capable of donating or accepting protons in solution.

Peptide bonds form when the carboxyl group of one amino acid reacts with the amino group of another, releasing a water molecule. It is a covalent linkage.

Peptide formation requires energy, usually supplied by the hydrolysis of a high-energy phosphate compound such as ATP.

Peptides are chains of amino acids linked by peptide bonds. The classification depends on the number of amino acids: 2-4, 4-10, 11-50.

Proteins that consist of a single polypeptide chain.

The unique three-dimensional structure of a protein, determined by its amino acid sequence.

A covalent bond formed by the reaction of two cysteine residues, helping to stabilize protein structure.

Nonpolar amino acids tend to be located in the protein's interior, interacting with other hydrophobic amino acids.

Interactions between polar groups, such as -COO- and -NH3+, in the protein's side chains.

The arrangement of multiple polypeptide chains, or subunits, into a functional protein complex.

Proteins that form long rodlike filaments, providing structural support.

Proteins that have a spherical shape, are water-soluble, and often involved in biological processes.

A protein with two subunits.

A protein with three subunits.

A protein with multiple subunits.

The unfolding and disorganization of a protein's structure, leading to loss of function.

The native form of a protein is its natural, functional state.

Factors like heat, UV radiation, and heavy metals can disrupt protein structure and cause denaturation.

Denaturation can lead to increased viscosity, decreased solubility, and loss of biological activity in proteins.

A connective tissue protein that forms strong fibers, providing structural support in bones, skin, tendons, and ligaments.

The process of adding sugar molecules (glucose and galactose) to collagen, specifically to hydroxylysine residues.

The precursor to collagen, containing additional peptide sequences that are later removed.

A process that strengthens collagen fibers by creating covalent bonds between lysine residues.

A condition caused by Vitamin C deficiency, leading to weakened collagen and impaired wound healing.

A highly elastic protein found in connective tissues such as lungs, blood vessels, and ligaments.

The cyclic structure formed by the cross-linking of four lysine residues in elastin, contributing to its elasticity.

An enzyme that inhibits the breakdown of elastin, preventing damage to elastic tissues.