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SBI4U1 > Unit 1 Test > Flashcards

Unit 1 Test Flashcards

1
Q

Hydrogen Bonds

A

Attractive force between a partially positive atom and a partially negative atom. Either N, O, or F

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2
Q

Chemical Reactions

A

Changing the arrangements of atoms and ions by breaking and forming chemical bonds

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3
Q

Dehydration

A
  • AKA Condensation reaction.
  • OH from one molecule and H from another break apart while the remaining atoms join together.
  • Results in one big molecule and water
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4
Q

Hydrolysis

A
  • Reverse condensation
  • H2O is added to one large molecule to break it apart
  • Water is added and two products are created
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5
Q

Neutralization

A
  • Acid and base added together.
  • Produce a water and a salt
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6
Q

Redox

A
  • Involves reduction and oxidization
  • Oxidization: Losing electrons
  • Reduction: Gaining electrons
  • No electrons=oxidized
  • Receives electrons=reduced
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7
Q

Properties of water

A

Water is a universal solvent

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8
Q

Water form

A

H molecules are closer together

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9
Q

Ice form

A

H molecules are further

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10
Q

Heat capacity

A
  • Amount of energy needed to raise the temperature.
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11
Q

Cohesion

A

What allows animals to walk on water

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12
Q

Adhesion

A

Allows water to stick to thinks (i.e. xylem)

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13
Q

Hydrophobic

A

Not attracted to water (non-polar)

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14
Q

Hydrophilic

A

Attracted to water (polar)

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15
Q

Amphipathic

A

Contains both polar and non-polar properties

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16
Q

Carbs
(monomer, functional group, bond)

A

Monomer: Monosaccharide
Functional group: Carbonyl and Hydroxyl
Bond: Glycosidic linkage

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17
Q

Alpha vs beta bonds

A

Alpha: OH is below the plane
Beta: OH is above the plane

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18
Q

Carb storage molecules

A

Starches
- Glycogen ans Cellulose

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19
Q

Lipids

A
  • Do not have a monomer
  • Non-polar
  • Fatty acids, fats, phospholipids, steroids, and waxes
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20
Q

Saturated vs Unsaturated

A

Saturated: All single bonds, unhealthy
Unsaturated: Some double bonds, healthy

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21
Q

Proteins

A

Monomer: Amino Acids
Functional groups: Amino group, carboxyl, and an R group
Bonds: Peptide bonds

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22
Q

Protein Structure

A
  1. Primary: Different amino acids are arranged accordingly to form a polypeptide chain
  2. Secondary: Chains are folded or coiled (alpha helix or beta pleated)
  3. Tertiary: 3D structure is determined based on the bonds and repulsion of the molecules composition
  4. Quaternary: Merging of 2 or more polypeptides
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23
Q

Denaturation

A

Temperature and pH can impact /alter a protein

24
Q

Nucleic acids

A

Monomer: Nucleotides
Structure: Nitrogenous base, phosphate group, and pentose
Functional group: Phosphate
Bond: Phosphodiester bond

25
Q

Pentose

A

RNA: Pentose is called Ribose (Ribonucleic acid)
DNA: Pentose is called deoxyribose
(deoxyribonucleic acid)

26
Q

Nitrogen Bases

A

Adenine, Thymine, Guanine, Cytosine, and Uracil
Thymine is only DNA
Uracil is only RNA

27
Q

Families of Nitrogen Bases

A

Pyrimidines: 6 membered and single ringed
(Cytosine, Thymine, and Uracil)

Purines: 5 and 6 membered joint together, double ringed (Adenine and Guanine)

28
Q

Enzymes

A

Biological catalyst, usually a protein, that changes the rate of a chemical reaction without being changed itself

Purpose: To speed up chemical reactions

29
Q

What is the activation energy for enzymes?

A

Typically it is heat, but too much can lead to denaturation

30
Q

Allosteric Inhibitor
(competitive vs non)

A

Competitive: Bind to the active site and prevent enzyme activity
Non-competitive: Bind somewhere else on the cell which changes the shape, also preventing enzyme activity

31
Q

Allosteric Activator

A

Binds to cell, changes its shape, enhancing enzyme activity (allows the substrate to attach)

32
Q

Feedback Inhibition

A

Prevention of wasting cellular resources being wasted by using excess product of an enzyme inhibitor to slow down production

33
Q

Substrate

A

Reactant substance that is recognized and binds to an enzyme. Tends to be small

34
Q

Active site

A

Specific pocket, grove, or indent in the enzyme where the substrate enters

35
Q

E.S complex

A

Process of an enzyme and substrate binding together

36
Q

Activation energy

A

Minimum amount of energy required to complete a chemical reaction

37
Q

Conformation

A

Enzymes are flexible molecules that change shape to better bind to substrates

38
Q

Co factor

A

Non protein group that binds to an enzyme such as Zn, Cu, or Fe and helps with chemical reactions

39
Q

Co enzymes

A

Organic co factors with similar jobs. Usually derived from water soluble vitamins

40
Q

Saturation level

A

Enzymes are saturated with substrates and new ones cannot bind to the active site until more enzymes become available

41
Q

Fluid Mosaic Model

A

Description used to explain the characteristic of the cellular membrane

42
Q

Lipid molecules
sat. vs. unsat.

A

Saturated: Fatty acids are closer together and the membrane becomes more rigid
Unsaturated: Fatty acids have kinks which make more space available in the membrane and makes it more fluid

43
Q

Sterols

A

AKA cholesterol
They are INSIDE the membrane
High temp: Restrain movement
Low temp: Occupy space to avoid forming a semisolid gel

44
Q

Main Molecules in Membrane

A

Glycolipid: Membrane lipid bound to a carb
Glycoprotein: Membrane component that contains a sugar and is bound to an amino acid
Phospholipid: 2 fatty acid tails linked to a glycerol, phosphate, and a compound

45
Q

Membrane Proteins

A

Help determine the specific function of the membrane

46
Q

4 types of membrane protein

A
  1. Transport
  2. Enzyme Activity
  3. Receptor
  4. Anchor
47
Q

The two types of membrane protein (in terms of placement on membrane)

A
  1. Transmembrane/integral: Embedded inside the membrane and interacts with the hydrophobic part
  2. Peripheral: Only on the surface, interacts with the hydrophilic part
48
Q

Passive Transport

A

Movement of molecules in biological systems that do NOT require energy

49
Q

3 Types of Passive Transport

A
  1. Simple diffusion: Substance moves across membrane unassisted
  2. Facilitated diffusion: Requires help from transmembrane proteins
  3. Osmosis: Movement of water in/out of cells
50
Q

Osmosis

A

Diffusion of water across a semipermeable membrane based on demand and concentration since the solute cannot move

51
Q

Explain Hypotonic, Hypertonic, and Isotonic

A

Hypotonic: Solution has less solute than the cell-causes the cell to swell
Hypertonic: Solution has more solute than cell-causes cell to shrivel
Isotonic: Equal solute, equal water. Perfect equilibrium

52
Q

Active Transport

A

Transportation across the membrane with the help of the cell’s energy to move materials in and out of the cell

53
Q

Exocytosis

A

Large molecules transported out of the cell with the help of the surrounding phospholipid bilayer engulfing the substances.
Exo=exit

54
Q

Endocytosis (and the 3 types)

A

Importing large molecules from the exterior of the cell to the cytosol

Pinocytosis: Cell brings in water or liquid (think pinot grigio)
Phagocytosis: Cell brings in solid particles (think “f” for food)
Receptor-mediated endocytosis: Outer cell contains surface receptor proteins that recognize and bind to specific molecules, bringing them into the cell

55
Q
A

SBI4U1 (1 decks)

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