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AP Biology > Biochemistry & Cells pt1 > Flashcards

Biochemistry & Cells pt1 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

What makes something organic?

A
  • carbon based molecule
  • complex, made by living things
  • carbon backbone
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2
Q

Dehydration synthesis

A

When forming polymers, H20 is released and energy is a reactant

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3
Q

Hydrolysis

A

When breaking polymers, H20 is a reactant and energy is a product (released)

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4
Q

The elements in carbohydrates include:

A

C, H, O

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5
Q

The ratio of elements in carbs (C, H, O)

A

1:2:1

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6
Q

What is the function of carbohydrates

A
  • Energy

- Structure

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7
Q

More specifically, carbs are needed because

A

They are a source of energy for your body and cells by breaking bonds and most give structure like cellulose and plant cell walls

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8
Q

Monosaccharide

A

The smallest carbohydrates; sugar

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9
Q

Polysaccharide

A

A chain of more than 10 linked monosaccharides like starch

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10
Q

Lipid

A

Nonpolar organic compounds such as oils and fats

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11
Q

What are the elements in lipids

A

C, H, O

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12
Q

How do lipid elements need to be balanced?

A

There are a lot more hydrogens and less oxygen making the ratio different than they are in carbohydrates. Oxygen is very electronegative and causes the lipid to be polar until H comes to balance it so it stays nonpolar (lipids are always non-polar)

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13
Q

Do lipids dissolve well in water?

A

No, they are hydrophobic (nonpolar)

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14
Q

Why do lipids have the most energy in them out of all the organic compounds?

A

Since they have a higher proportion of C and H, there are a lot of C-H bonds which are high in energy able to be extracted from them.

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15
Q

What do lipids do?

A

1) Energy molecules (C-H bonds can make ATP)
2) Basis of membranes (line up to form border of cell)
3) Involved in signaling (some hormones fall into the lipid category b/c nonpolar)

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16
Q

Types of Lipids:

A

Fat, Steroids, Phospholipids

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17
Q

(Lipid) Fat

A
  • have fatty acid tails
  • long tails with lots of C-H bonds
  • have glycerol
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18
Q

(Lipid) Steroid

A
  • 4 ring base structure
  • some are hormones
  • hormones have special properties (non polar) that make them able to go through membrane or side of a cell
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19
Q

Phospholipid

A
  • similar to fats
  • added phosphate group on glycerol
  • creates membranes
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20
Q

1) Headgroups (glycerol & phosphate):

2) Tails:

A

1) polar

2) nonpolar

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21
Q

What molecules pass through the cell membrane?

A

Non polar because they make up the majority of the inside of the membrane

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22
Q

What elements are in nucleic acids?

A

C, H, O, N, P (yum)

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23
Q

monomer for nucleic acid is

A

nucleotide

24
Q

What do nucleic acids do?

A

Provide instructions on how something produces proteins

25
Q

Structure of NA

A
  • phosphate
  • sugar molecule
  • nitrogenous base (DNA*)
26
Q

RNA vs DNA

A

RNA

  • single strand
  • Uracil
  • ribose sugar

DNA:

  • double strand
  • Thymine
  • deoxyribose sugar
27
Q

When can you calculate rate?

A

If time is on the x axis

28
Q

All molecules made by a cell contain what

A

Carbon chains

29
Q

are organic molecules big?

A

Very massive (macromolecule)

30
Q

Anabolism

A

A metabolic reaction in which complicated molecules are built from simpler ones, energy is required.

31
Q

Catabolism

A

A metabolic reaction in which energy is released through the breakdown of complex molecules into simpler ones.

32
Q

Coenzyme

A

An organic compound necessary for the functioning of an enzyme.

33
Q

Cofactor

A

An organic or inorganic molecule necessary for an enzymatic reaction to take place (wingman)

34
Q

Why are proteins unique?

A

They all have more complex structures that makes them able to have more functions

35
Q

Structure of a protein

A
  • Carbon backbone that goes 4 directions
  • Amino group that has 1N and 2H
  • Carboxyl group connected to central carbon
  • Hydrogen group
  • “R-Group” is a variety of things
36
Q

Amino group and carboxyl groups cant be bonded to themselves so…

A

They bond with each other

Amino group + Carboxyl 4everrr

37
Q

When bonding amino acids what do you do?

A

Remove H20 b/c its dehydration synthesis

38
Q

How many different R groups are there

A

20

39
Q

What would changing AA order do

A

change the proteins shape and function

40
Q

R group interactions form what

A

3D tertiary structure to proteins

41
Q

More than 1 polypeptide with a beginning and an end indicates:

A

4th level structre

42
Q

What are disulfide bonds?

A

Covalent bonds

43
Q

Hydrogen bonds?

A

2 polars coming together with partial charges

44
Q

Protein vs polypeptide

A

Protein is the FINISHED product with all its polypeptides in completed chains

45
Q

Folding of proteins:

A

1) hydrogen bonding occurs from amino group (its H) and carboxyl group <3 (its O)
2) Positive and negative interactions have ionic pull on eachother

3 )NP and NP go in the middle bc likes go w likes

46
Q

Amino acids held together by:

A

Peptide bonds

47
Q

Why will a line slow down in a graph with time and amount of product?

A

Because eventually you will run out of substrates and just have products

48
Q

Graph with substrate concentration on the X-Axis and rate of reaction on the Y-axis

A
  • More substrates increases the rate of reaction
  • When every enzyme is filled by a substrate (SATURATED) the rate will become constant because no more reactions can occur
49
Q

Graph with enzyme concentration on the x-axis and rate of reaction on the y-axis

A
  • As you increase enzyme concentration, the rate of reaction increases
  • There are always extra substrates, so the more enzymes added, the rate will always increase
50
Q

Feedback Inhibition/Negative Feedback

A

When you stop the first enzyme and the rest of the reaction using a product to do so

51
Q

Coenzymes

A

They are an organic portion of a protein that is an additional chemical attached to help the enzyme do its job

  • carbon
  • vitamins
52
Q

Cofactors

A
  • found in some enzymes
  • essential to function
  • inorganic
  • metals (charged)
53
Q

Inhibitors

A
  • slows down the reaction

- stops f(x)

54
Q

Competitive inhibitors

A

-Similar shape to substrate so it will also go into the ACTIVE SITE and block the reaction

55
Q

Noncompetitive inhibitors

A
  • Goes to the ALLOSTERIC site located somewhere in the protein
  • changes protein and active site shape so substrates can’t fit
56
Q

Activators

A
  • change a protein shape if its wrong to the right one so it can function
  • Allosteric site
57
Q

Enzymes

A
  • work faster at higher temperatures bc enzymes collide and at low temps, they move slow
  • If they get too high (past 98 degrees F) they denature and don’t function
  • Work best at a pH of 7 because that’s neutral and acidic or basic environments have too many H+ or OH-

AP Biology (5 decks)

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