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Biochemistry Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Define Cohesion vs Adhesion

A

Cohesion: molecules bonding to each other (H20-> H20)
Adhesion: molecules bonding to other substances (H20->CO2)

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2
Q

What type of molecule is water? How does it bond to other water molecules?

A

Water is Polar Covalent. It bonds to other water molecules through hydrogen bonding (dipole-dipole)

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3
Q

Define surface tension. Describe how hydrogen bonds affect surface tension.

A

Surface tension: the ability of a substance to withstand external force. The stronger the intermolecular force (eg. hydrogen bonds, in terms of water) the higher the surface tension.

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4
Q

How does water’s surface tension change when a nonpolar substance is added? (eg. soap, oil)

A

Surface tension LOWERS, hydrogen bonds are broken. Water becomes less cohesive.

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5
Q

Give one example (NOT the nickel) of the cohesive and adhesive properties of water.

A

Transpiration in plants: water clings to and moves through the xylem and phloem.

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6
Q

How do you identify an alcohol?

A

Hydroxyl group (OH) attached to a carbon chain.

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7
Q

How do you identify an aldehyde?

A

A carbonyl group (carbon doubled bonded to O, single bond to H)

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8
Q

How do you identify a ketone?

A

Carbon double bonded to O.

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9
Q

How do you identify a carboxylic acid?

A

A carboxyl group (carbon double bond to O, single bond to OH)

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10
Q

How do you identify an amine?

A

An amino group (N bonded once to 2 separate H, NH2)

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11
Q

How do you identify an amide?

A

Carbon, double bond to O, single bond to NH2.

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12
Q

What element is the building block of life?

A

Carbon

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13
Q

How many bonds can carbon have?

A

Four.

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14
Q

A biological catalyst is also called an _________

A

Enzyme.

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15
Q

In biology, useful molecules must be ________ so they can be carried around by __________.

A

Polar, water.

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16
Q

Define STRUCTURAL Isomer

A

A compound that has the same number of the same atoms (eg. 4 carbon) bonded in a different arrangement.

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17
Q

Define a GEOMETRIC isomer.

A

A molecule that has the same atoms, but varies in arrangement around a double bond. Will produce either a cis-isomer or a trans-isomer, depending on if the functional groups are on the same side or opposites

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18
Q

Define a polymer. What are polymers made of?

A

A polymer is a very large molecule consisting of smaller repeating subunits, called monomer. (eg. Starch is a polymer, but glucose is a monomer)

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19
Q

What is the difference between alpha and beta glucose?

A

Alpha glucose is a cis-isomer (hydroxyl groups), beta glucose is a trans-isomer.

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20
Q

What do glucose molecules join to form in PLANTS?

A

Alpha-glucose —> starch
Beta-glucose —> cellulose

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21
Q

What do glucose molecules join to form in ANIMALS?

A

Alpha-glucose—> glycogen (food storage)

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22
Q

Define Cellulose.

A

Major structural material of all plants, straight and tightly packed chains. Cannot be digested. Made of beta-glucose.

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23
Q

Define starch.

A

Stores energy. Forms branched chains. Can be digested, made of alpha-glucose.

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24
Q

Give two examples of Monosaccharides (not alpha or beta).

A

Galactose - sugar in milk.
Fructose - sugar in honey.

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25
Q

Give three examples of disaccharides.

A

Maltose, lactose, sucrose.

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26
Q

Give four examples of polysaccharides.

A

Glycogen, starch, cellulose, chitin.

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27
Q

The link between two glucose molecules is called a ______.

A

Glycosidic link.

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28
Q

Name the four isomers of C6H12O6

A

Alpha-glucose, beta-glucose, fructose, galactose.

29
Q

Define an OPTICAL isomer

A

An isomer that is a non-superimposed mirror image of itself around its center.

30
Q

Proteins are ______, and Amino Acids are ________.

A

Polymers, monomers.

31
Q

How many amino acids are there in the human body? Which is the simplest?

A

20 different amino acids, and glycine is the simplest.

32
Q

What TWO functional groups do every single amino acid contain?

A

Carboxyl group (double bond to O, single bond to OH) and an amino group (NH2).

33
Q

When two amino acids join together, they form a _______ and connect through a _________.

A

Dipeptide, peptide bond.

34
Q

What type of reaction forms dipeptides? Are there any byproducts?

A

Condensation reaction, water byproduct.

35
Q

Name the four functions of proteins.

A
  1. Biological catalysts (enzymes)
  2. Provide structure (eg. Muscle, skin)
  3. Cell signalling/recognition
  4. Molecules of immunity
36
Q

What is the structural difference between saturated and unsaturated lipids?

A

Saturated - full of hydrogen bonds
Unsaturated - not full of hydrogen (due to double bonds)

37
Q

Name one properties of saturated fatty acids and why it behaves as such

A

Solid at room temperatures, because the straight molecular chains can pack tightly together.

38
Q

Name one property of unsaturated fatty acids and why they behave as such.

A

Liquid at room temperature, as the bent chain cannot pack tightly.

39
Q

What type of lipid is the major component of all cell membranes?

A

Phospholipids

40
Q

What are the two types of nucleic acid?

A

Deoxyribonucleic acid (DNA) and ribonucleic acid (RNA).

41
Q

Lactose is made from which two isomers of glucose?

A

Alpha-glucose and galactose.

42
Q

Sucrose is made from which two isomers of glucose?

A

Alpha-glucose and fructose.

43
Q

Maltose is made from which two isomers of glucose?

A

Alpha-glucose and alpha-glucose.

44
Q

A triglyceride is made up of what?

A

A glycerol and three fatty acids.

45
Q

How does the structure of a phospholipid differ from a triglyceride?

A

Triglyceride: glycerol + 3 fatty acids
Phospholipid: glycerol + 2 fatty acids + phosphorus

46
Q

What are the three essential parts of a nucleotide?

A

A phosphate group, a (pentose) sugar, and a nitrogenous base.

47
Q

What is the chemical formula of maltose and why is it unusual?

A

C12H22O11 - double glucose, but missing two hydrogen and one oxygen because water is released (H2O).

48
Q

What type of bond is it when the sugar of one nucleotide bonds with the phosphate of another?

A

A (polar) covalent bond.

49
Q

When creating a helix structure, what type of bond occurs between two nucleotides’ nitrogenous bases?

A

Hydrogen bond

50
Q

What are the 2 difference between DNA’s structure and RNA’s structure?

A

Strands: DNA is double-stranded, RNA is single-stranded
Sugar: DNA’s pentose sugar is deoxyribose, RNA’s pentose sugar is ribose.

51
Q

Define oligosaccharide.

A

Carbohydrates that contain between two and ten monosaccharides, and may contain any of the four glucose isomers.

52
Q

The four common carbohydrate polymers are starch, cellulose, glycogen, and chitin. For each, where are they found, how are they made, and what is their use?

A

Starch: plants, alpha-glucose, stores energy.
Cellulose: plants, beta-glucose, structural integrity
Glycogen: animals, glucose monosaccharides, glucose storage
Chitin: mainly fungi, fructose/galactose, strength within cellular structures

53
Q

What makes a complete protein?

A

Contains the nine amino acids the human body cannot produce.

54
Q

Glycogen, a polysaccharide, is used to store glucose. What makes its structure so unique?

A

It is branched, like a tree’s root web, to allow for higher water solubility.

55
Q

Fructose is WHAT TYPE of isomer?

A

Structural.

56
Q

Enzymes are named very simply. For example, the enzyme that processes lactose is called ________, the enzyme that processes maltose is called ______.

A

Lactase, maltase.

57
Q

Enzymes _______ the activation energy of a reaction, _____________ the speed of the process.

A

Decrease, increasing

58
Q

Describe an enzyme’s primary structure.

A

Hundreds or thousands of amino acid chains, forming peptide bonds (amino end of one to the hydroxyl end of another) and becoming polypeptides

59
Q

Describe an enzyme’s secondary structure

A

Folding of the polypeptide into spirals or pleated sheets. Caused by HYDROGEN BONDS, forming between carbonyl and amine groups on the amino acids.

60
Q

Describe the tertiary structure of an enzyme

A

Defines the overall 3D shape, based on interactions between side groups of the peptide chain (hydrogen or disulfide bonds).

61
Q

Describe the quaternary structure of an enzyme

A

When two or more polypeptides join together to form a folded, globular protein. Held together through hydrogen bonding.

62
Q

Name and define the three types of enzyme inhibition.

A

Competitive: bonds to active site.
Non-competitive: bonds to allosteric site, changes shape of enzyme
Non-specific: causes changes to denature enzymes (heat, pH)

63
Q

Describe the structure of a phospholipid and name where it is found.

A

Phosphate ‘head’ (attracted to water) and fatty acid ‘tail’ (repelled from water). Found in the cell membrane - phospholipid bilayer!

64
Q

Name the four main membrane components and their function

A

Cholesterol: maintains fluidity, spaces out phospholipids
Integral proteins: act as channels for large molecules
Peripheral proteins: protein marker, identify receptors on the membrane
Glycolipids/proteins: interactions w other cells, signalling within the cell.

65
Q

Define active vs passive transport

A

Active transport requires ATP (energy) - molecules move against a concentration gradient. Passive transport requires no energy, moves with the gradient.

66
Q

Define solute vs solvent.

A

Solute: molecule that can dissolve.
Solvent: liquid that can dissolve molecules.

67
Q

What are the three types of passive transport?

A

Diffusion, facilitated diffusion, and osmosis.

68
Q

Isotonic vs hypotonic vs hypertonic OSMOTIC SOLUTIONS

A

Isotonic - same amount of solute/water inside/outside the cell.
Hypotonic - less solute, more water OUTSIDE
hypertonic - more solute, less water OUTSIDE

Biology (6 decks)

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