Biochemistry Concepts Quiz

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

<p>100 times (A)</p> Signup and view all the answers

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

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

<p>As the pH increases, the hydrogen ion concentration decreases. (B)</p> Signup and view all the answers

<p>MgCl2 (B)</p> Signup and view all the answers

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

<p>To act as messengers in the immune and nervous systems. (D)</p> Signup and view all the answers

<p>A molecular formula shows the types and numbers of atoms in a molecule, while a structural formula shows the arrangement of atoms in a molecule. (D)</p> Signup and view all the answers

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

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

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

<p>When the balance of ions in the blood is disrupted, either too high or too low. (C)</p> Signup and view all the answers

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

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

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

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

<p>To become more stable (C)</p> Signup and view all the answers

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

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

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

<p>Beta-pleated sheet (C)</p> Signup and view all the answers

<p>The final three-dimensional shape of a polypeptide chain (D)</p> Signup and view all the answers

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

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

<p>It terminates or disturbs the activity (C)</p> Signup and view all the answers

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

<p>Proteins contain amino acid monomers linked by peptide bonds. (B)</p> Signup and view all the answers

<p>A nonprotein structure that can bind to proteins (D)</p> Signup and view all the answers

<p>A structure formed by two amino acids bonded together. (A)</p> Signup and view all the answers

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

<p>They determine the amino acid's identity. (C)</p> Signup and view all the answers

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

<p>Creation of peptide bonds between amino acids. (C)</p> Signup and view all the answers

<p>20 (B)</p> Signup and view all the answers

<p>The specific arrangement and interaction of their structures. (A)</p> Signup and view all the answers

<p>They have R groups that include elements like O, N, or S. (D)</p> Signup and view all the answers

<p>Glutamic acid and aspartic acid. (B)</p> Signup and view all the answers

<p>It forms disulfide bridges stabilizing protein structure. (D)</p> Signup and view all the answers

<p>Four: primary, secondary, tertiary, and quaternary. (B)</p> Signup and view all the answers

<p>They assist in the proper folding of proteins. (A)</p> Signup and view all the answers

<p>The linear sequence of amino acids. (D)</p> Signup and view all the answers

<p>Covalent bonding. (B)</p> Signup and view all the answers

<p>Its R group attaches to the amino group, forming a ring. (D)</p> Signup and view all the answers

Maintaining homeostatic blood levels of ions for optimal health.

When blood ion concentrations are too high or too low.

Bond formed by the electrostatic attraction between cations and anions.

Ionic compounds formed from the bonding of cations and anions.

A positively charged ion, formed by donating an electron.

A negatively charged ion, formed by gaining an electron.

A bond formed when atoms share electrons.

Compounds made of two or more different elements bonded covalently.

Lipid molecules with a four multi-ring structure, important in biology.

Modified 20-carbon fatty acids involved in inflammation and communication.

Lipids with carbohydrates attached, crucial for cell membrane functions.

Vitamins A, E, and K, which dissolve in fats.

The simplest form of carbohydrate, a single sugar unit.

Two monosaccharides bonded together, forming a simple sugar.

Long chains of monosaccharides, serving as energy storage.

The regulation of blood sugar levels by hormones and processes.

Molecules with both polar and nonpolar regions, dissolving partially in water.

A water molecule with an extra hydrogen ion, representing acidity.

A water molecule that has lost a hydrogen ion, indicating basicity.

A solution with a higher concentration of H⁺ ions, pH below 7.

A solution with a higher concentration of OH⁻ ions, pH above 7.

A measure of hydrogen ion concentration, ranging from 0 to 14.

An acid that completely dissociates in water, producing many H⁺ ions.

A solution with equal concentrations of H⁺ and OH⁻, pH of 7.

Polymers made of amino acid monomers with diverse functions.

Building blocks of proteins, consisting of carboxyl and amine groups.

Side-chain structures in amino acids that determine their properties.

Covalent bond linking amino acids, formed via dehydration synthesis.

Functions include enzymes, transport, defense, and storage.

Dipeptide: 2 amino acids; Polypeptide: 3-200 amino acids linked.

Proteins covalently bonded to carbohydrates; crucial for cell identification.

Amino acids are grouped as nonpolar, polar, charged, or special.

Amino acids with R groups containing O, N, or S that interact with polar molecules and water.

Amino acids that carry either a positive or negative charge.

Amino acids such as glutamic acid and aspartic acid with a negatively charged R group.

Amino acids like histidine, lysine, and arginine with a positively charged R group.

An amino acid whose R group connects to the amino group, creating a ring structure.

An amino acid containing a sulfhydryl group, forming disulfide bonds to stabilize proteins.

The first amino acid in protein synthesis, always initiating the polypeptide chain.

Four levels of protein structure: primary, secondary, tertiary, and quaternary.

Weak attractions between polar R groups or amine and carboxylic groups in amino acids.

Covalent bonds formed between the sulfhydryl groups of two cysteine amino acids.

Repeating patterns in protein, primarily alpha helix and beta-pleated sheet.

A coiled structure in proteins providing elasticity, often found in fibrous proteins.

A flat, folded structure in proteins offering flexibility found in globular proteins.

The overall three-dimensional shape of a single polypeptide chain.

Loss of protein structure due to nonoptimal chemical conditions like pH or temperature.