bio

Question 1

what are Atoms:

Answer 1

Atoms: Single unit made up of neutrons,
protons, and electrons

Question 2

what are Molecule:

Answer 2

Groups of 2+ atoms held
together by chemical bonds due to
electron interactions

Question 3

what are Macromolecules:

Answer 3

Large molecules
(polymers) formed from the bonding of
smaller molecules (monomers)

Question 4

what is an ionic bond

Answer 4

an ionic bond is a transfer of energy from one atom to an other of a very different electronegativity

Question 5

what is a covalent bond

Answer 5

Sharing of e- between atoms of similar
electronegativities
* Nonpolar: equal e- sharing
* Polar: unequal e- sharing, forms dipole

Question 6

what is a hydrogen bond

Answer 6

Bonds: Weak bond between a hydrogen atom
and an electronegative atom (F, O, or N)

Question 7

what is a

Answer 7

Links monomers to form
polymers, forming H2O in the process

Question 8

what is Hydrolysis:

Answer 8

Uses water to break polymers into
monomers

Question 9

background information of a protein: Monomer, polymer, linkage type, function

Answer 9

Monomer: Amino acid
* Polymer: Peptide
* Linkage type: Peptide bonds
* Function: Structure, transport,
defense, storage, enzymes

Question 10

what are the Protein Structures and explanation of each

Answer 10

1. Primary: Linear chain
   sequence of amino acids
2. Secondary: Local folding of
   chain into α-helices/β-sheets
   via H-bonding between
   amino & carboxyl groups of
   adjacent amino acids
3. Tertiary: 3D shape due to
   noncovalent interactions
   between R groups
4. Quaternary: 3D protein
   shape consisting of 2+
   separate peptide chains

Question 10

what are the Protein Structures and explanation of each

Answer 10

1. Primary: Linear chain
   sequence of amino acids
2. Secondary: Local folding of
   chain into α-helices/β-sheets
   via H-bonding between
   amino & carboxyl groups of
   adjacent amino acids
3. Tertiary: 3D shape due to
   noncovalent interactions
   between R groups
4. Quaternary: 3D protein
   shape consisting of 2+
   separate peptide chains

Question 10

what are the Protein Structures and explanation of each

Answer 10

1. Primary: Linear chain
   sequence of amino acids
2. Secondary: Local folding of
   chain into α-helices/β-sheets
   via H-bonding between
   amino & carboxyl groups of
   adjacent amino acids
3. Tertiary: 3D shape due to
   noncovalent interactions
   between R groups
4. Quaternary: 3D protein
   shape consisting of 2+
   separate peptide chains

Question 11

background information of a Carbohydrates: Monomer, polymer, linkage type, function

Answer 11

Monomer: Monosaccharide
Polymer: Polysaccharide
Linkage type: Glycosidic
Function: Store energy

Question 12

Classes of Carbohydrate and description

Answer 12

Monosaccharides: Single
sugar molecule (e.g., Glucose)

Disaccharides: 2 joined sugar
molecules (e.g., Glucose +
Fructose = Sucrose)

• Polysaccharides: Polymer of
  sugar molecules. Includes
  starch (α-glucose), glycogen
  (α-glucose), cellulose (β-
  glucose), chitin (β-glucose)

Question 13

background information of a lipids : Monomer, polymer, linkage type, function

Answer 13

Nonpolar, hydrophobic molecules
* Monomer: Hydrocarbons
* Polymer: Hydrocarbon chain
* Linkage type: Covalent carbon-carbon
* Function: Insulation, energy storage, endocrine signalling and cell structure

Question 14

Types of Lipids

Answer 14

1. Triglycerides: Glycerol + 3 fatty acids
   * Saturated (single bonds, straight chain)
   * Unsaturated (double bonds, branched chain)
2. Phospholipids: 2 fatty acids +
   phosphate group attached to glycerol
   backbone
   * Are amphipathic with polar head, nonpolar tail.
   * Form phospholipid membrane bilayer
3. Steroids: Three 6-membered rings +
   one 5-membered ring * E.g., hormones, cholesterol
4. Porphyrins: 4 joined pyrrole rings with
   a metal center atom
   * E.g., chlorophyll, hemoglobin