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SBI 4UI > Unit 1: Biochemistry > Flashcards

Unit 1: Biochemistry Flashcards

1
Q

isotope

A

a form of an element that differs in its number of neutrons

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2
Q

valence electron

A

an electron in the outermost energy level or shell of an atom

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3
Q

ionic bond

A

a bond that results from the attraction between 2 oppositely charged atoms or molecules

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4
Q

covalent bond

A

atoms that share one or more valence electrons

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5
Q

hydrogen bond

A

the attractive force between a partially + charged hydrogen atom and a partially - charged atom in another molecule

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6
Q

Van der Waals force

A

very weak attractions between 2 molecules or part of molecules, when they are close together

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7
Q

electronegativity

A

the measure of an atom’s attraction to shared electrons

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8
Q

intermolecular forces

A

the force of attraction between 2 molecules

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9
Q

dehydration synthesis

A

a chemical reaction in which subunits of a larger molecule are joined by the removal of water (aka condensation reaction)

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10
Q

hydrolysis

A

a chemical reaction in which water is used as a reactant to split a larger molecule into smaller subunits

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11
Q

oxidation

A

a reaction in which a molecule loses electrons

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12
Q

reduction

A

a reaction in which a molecule gains electrons

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13
Q

List 4 characteristics unique to water that are due to its chemical structure

A
  1. Solid water is less dense than liquid (it floats)
  2. Water has high boiling point (most water on Earth is in liquid form rather than gas)
  3. Water clings to itself and some other molecules
  4. Many substances dissolve in water
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14
Q

autoionization

A

the process in which a molecule spontaneously dissociates into ions

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15
Q

acid

A

characterized by sour taste, conductivity, turn litmus paper red

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16
Q

base

A

characterized by bitter taste, slippery, conductivity, turn litmus paper blue

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17
Q

neutralization

A

when an acid and base react with one another, water and salt are produced

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18
Q

buffer

A

a chemical that compensates for pH change in a solution by accepting or donation H+ ions

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19
Q

hydrophobic

A

non-polar molecules that are not strongly attached/attracted to water

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20
Q

hydrophilic

A

polar or charged molecules that are strongly attracted to water

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21
Q

adhesion

A

water molecules form hydrogen bonds with other polar molecules

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22
Q

cohesion

A

water molecules form hydrogen bonds with each other

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23
Q

List the 3 types of sugars and examples.

A

Monosaccharide - simple sugars (i.e, glucose, fructose)
Disaccharide - 2 simple sugars linked together (i.e, sucrose made by linking glucose and fructose)
Polysaccharide - many simple sugars linked together (i.e, starch, glycogen, cellulose)

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24
Q

How are sugars linked together?

A

dehydration reaction

25
Q

Why do carbohydrates dissolve well in water but lipids do not?

A

Carbohydrates are made of C,H,O atoms where many O-H bonds are polar.
Lipids are made of C,H,O atoms where many C-H bonds are non-polar.

26
Q

How is a phospholipid formed?

A

One of the 3 fatty acids are replaced by a phosphate group

27
Q

Characteristics of saturated fats

A
  • Hold as much hydrogen as possible
  • Solids at room temp.
  • Molecules are flat and stack closely together
28
Q

Characteristics of unsaturated fats

A
  • Do not hold as much hydrogen as they could
  • Liquids at room temp
  • Molecules bend and do not stack evenly
29
Q

What makes the shape of saturated and unsaturated fats significant?

A

Saturated fats are flat and line the blood vessels more easily, whereas unsaturated fats are bent and enzymes are able to get between them and break them down.

30
Q

CIS fats

A

Unsaturated fats that occur naturally and are bent

31
Q

TRANS fats

A

Artificially created unsaturated fats that are flat

32
Q

What atoms are proteins made out of?

A

C, H, O, N, (S) atoms

33
Q

What are amino acids and what gives them their distinct characteristics?

A

Amino acids are the building blocks of proteins; variable regions (“R groups”) give them their distinct characteristics.

34
Q

What are enzymes?

A

Enzymes are molecules that speed up the rate of reactions in biological systems.

35
Q

How do enzymes work?

A

Enzymes bind to substrates, lowering the energy of activation using a “lock and key” method.

36
Q

What is the “lock and key” method?

A

The substrate must fit exactly into the active site on the enzyme and its reaction speeds up.

37
Q

What are competitive inhibitors?

A

Substances that enter the active site on the enzyme, keeping the normal substrate from binding. (compete for a spot on the enzyme)

38
Q

What are non-competitive inhibitors?

A

Substances that bind to an area on an enzyme other than the active site, changing the shape of the enzyme and affecting the active site.

39
Q

What is the allosteric site on an enzyme?

A

A binding site on an enzyme that binds regulatory molecules; changes the shape of the enzyme and affects the active site

40
Q

allosteric regulation

A

The regulation of one site of a protein by binding to another site on the same protein

41
Q

Difference between active transport and passive transport through the cell membrane

A

Passive: movement of particles using no energy (diffusion, osmosis, facilitated diffusion)
Active: movement of particles against concentration gradient (from low to high), requiring ATP energy

42
Q

List the 4 main classes of biological molecules.

A

Carbohydrates, proteins, lipids and nucleic acids

43
Q

What distinguishes saturated fats from unsaturated fats?

A

Types of covalent bonds (unsaturated has double bond)

44
Q

allosteric site

A

the binding site of regulatory molecules on an enzyme (that’s not the active site)

45
Q

How does allosteric regulation work?

A

Allosteric activation: allosteric activator allows substrate to fit into active site easier
Allosteric inhibition: allosteric inhibitor prevents substrate from fitting into active site

46
Q

Describe phagocytosis

A

a type of endocytosis that takes in large

particles

47
Q

Which term refers to the series of interacting organelles between the nucleus and the plasma membrane?

A

endomembrane system

48
Q

T/F: Only eukaryotic cells have mitochondria.

A

True

49
Q

T/F: Mitochondria and chloroplasts have evolved from

cells that were engulfed by other cells.

A

True

50
Q

Primary structure of proteins

A

Linear sequence of amino acids in a polypeptide chain

51
Q

Secondary structure of proteins

A

The specific coiling/folding of a protein; shapes held by hydrogen bonds; backbone interactions

52
Q

Tertiary structure of proteins

A

Overall 3 dimensional shape of the protein; cause by chemical interactions between R groups of amino acids

53
Q

Quaternary Structure

A

highly complex molecule formed when two protein chains interact with one another; held together by ionic bonds, H bonds, disulphide bridges

54
Q

Functions of glycoproteins in the fluid mosaic model

A
  1. Gatekeeper
  2. receptor for chemical messenger
  3. Identification
55
Q

What the difference between the bonds in saturated and unsaturated fats?

A

Saturated: single bond in hydrocarbon chain
Unsaturated: double bonds

56
Q

List the different solutions used for testing macromolecules.

A

Carbohydrates - Benedict’s
Starch - Lugol’s/Iodine
Protein - Biuret

57
Q

Endomembrane system

A

interacting organelles between the nucleus and the plasma membrane

58
Q

How would a glucose molecule move through the cell membrane?

A

Binds to a carrier protein and moves through the membrane through facilitated diffusion

SBI 4UI (6 decks)

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