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biochemistry terms Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

what percent of an organism is water?

A

90%

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2
Q

what is the universal solvent?

A

water

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3
Q

what are the properties of water?

A

Surface tension
Polar
Cohesive
Adhesive

SPCA

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4
Q

organic chemistry

A

the study of carbon-based molecules.

Although a cell is mostly water, the rest of the cell consists mostly of carbon based molecules.

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5
Q

electrons in a carbon atom

A

It has four electrons in an outer shell that holds eight.

It can share its electrons with other atoms to form up to four covalent bonds.

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6
Q

hydrocarbons

A

The simplest carbon compounds contain only carbon and hydrogen atoms

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7
Q

what do organic molecules always contain

A

Always contain carbon and hydrogen;

Almost always contain oxygen;

Often contain nitrogen or phosphorus. (or sulfur)

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8
Q

functional group

A

groups of atoms that give properties to the compounds to which they attach.

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9
Q

macromolecules

A

large molecules

carbohydrates, lipids, proteins, nucleic acids

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10
Q

polymers

A

a type of macromolecule

made by stringing together many smaller molecules (monomers)

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11
Q

monomers

A

smaller molecules

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12
Q

Dehydration synthesis

A

also known as CONDENSATION

links monomers by removing a molecule of water for every bond made.

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13
Q

hydrolysis

A

breaks down macromolecules, adding a molecule of water for each bond broken.

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14
Q

categories of large molecules in cells

A

Carbohydrates, Lipids, Proteins, Nucleic Acids

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15
Q

carbohydrates

A

sugars

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16
Q

MONOSACCHARIDES

A

monomer carbohydrates

simple sugars

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17
Q

common monosaccharides

A

glucose (blood sugar)

galactose (in milk sugar)

fructose (fruit sugar)

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18
Q

what do monosaccharides form in aqueous solutions

A

aqueous=watery

form rings structures (in cells!)

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19
Q

disaccharides

A

Larger sugars/smaller polymers

double sugar

2 monomers (rings) are bonded by dehydration synthesis

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20
Q

common disaccharides

A

sucrose (table sugar)

lactose (milk sugar)

maltose (grain sugar)

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21
Q

Polysaccharides

A

Large polymers

complex carbohydrates

Multiple monomers (rings) are bonded together to form chains of rings

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22
Q

examples of polysaccharides

A

starch (NRG storage in plants)

cellulose (structure in plants – the most abundant organic molecule on Earth!)

glycogen (NRG storage in animals)

23
Q

lipid functions

A

functions:
- energy storage
- help to insulate the body,
- cushions and protect organs

are hydrophobic –” water fearing”

24
Q

types of lipids

A

Steroids
Waxes
Oils
Fats

SWOF

25
Q

types of fatty acids

A

o Unsaturated fatty acids

o Saturated fatty acids

26
Q

unsaturated fatty acids

A

less than the maximum number of hydrogens bonded to the carbons (a double bond between carbons)

Most plant oils tend to be low in saturated fatty acids & exist as liquid at room temperature (oils)

27
Q

saturated fatty acids

A

have the maximum number of hydrogens bonded to the carbons (all single bonds between carbons)

Most animal fats have a high proportion of saturated fatty acids & exist as solids at room temperature

(butter, margarine, shortening = fats)

28
Q

Triglyceride

A

Composed of glycerol and three fatty acid chains

Glycerol forms “the backbone” of fat

Considered to be a large component of dietary fat

29
Q

Steroids

A

The carbon skeleton of steroids is bent to form 4-fused rings

30
Q

examples of Waxes

A

thin layer of coating on leaves and some fruits,

honeybee wax,

ear wax, etc

31
Q

Protein purpose

A

used to build cells, act as hormones & enzymes, and do much of the work in a cell

32
Q

four types of proteins

A

Structural,

Storage

Transport,

Contractile (muscular),

SSTC

33
Q

what are the monomers which make up proteins

A

All proteins are polymers made of monomers called AMINO ACIDS, linked in different orders

34
Q

Structure of amino acids

A

a central carbon with 4 things bonded to it:

i. Hydrogen -H
ii. Amino group -NH2
iii. Carboxyl group -COOH
iv. R group ( side group/radical – this is what defines each amino acid; what makes it unique)

........H
.........|
A -- C -- carboxyl
.........|
........R
35
Q

how and why do cells link amino acids together

A

to make proteins

by condensation and a peptide bond forms between each 2 amino acids in a the peptide chain

36
Q

Dipeptide

A

two amino acids

37
Q

Polypeptide

A

more than two amino acids

38
Q

what makes up protein

A

many polypeptide

39
Q

cholesterol

A

is the “base steroid” from which your body produces other steroids

40
Q

types of steriods

A

Estrogen and testosterone are also steroids

Synthetic Anabolic Steroids are variants of testosterone and cause many adverse problems.

41
Q

monomers that make up nucleic acids

A

nucleotides

42
Q

what makes up a nucleotide?

A

5-carbon, sugar, a phosphate group, and a nitrogenous base (? check)

43
Q

Polyunsaturated fatty acid

A

a lipid which has TWO OR MORE double bonds between the carbon atoms.

44
Q

what is an enzyme?

A

globular proteins which act as catalysts (speeds up reactions without being changed themselves)

45
Q

how do enzymes control the rate of chemical reactions?

A

by weakening bonds, lowering the amount of activation energy or EA (the initial amount of energy needed to start a reaction) needed for the reaction.

46
Q

what factors affect reaction rate?

A

temperature

pH

concentration of enzyme or substrate

47
Q

denaturation

A

changing the structure of an enzyme (or other protein), usually temporary, so that it can no longer carry out its function.

This change may be permanent (coagulation).

48
Q

lock and key enzyme activity

A

Molecules of the substrate fit the active site and are chemically attracted to it.

(kinda like a “perfect fit” I think)

49
Q

Induced fit

A

The substrate binds to the active site.

The enzyme “folds” around the substrate inducing bond strain on the substrate.

This bond strain reduces activation energy and reaction proceeds at a faster rate.

50
Q

competitive inhibition

A

the inhibitor competes for the ACTIVE SITE of the enzyme.

A competitive inhibitor occupies the active site temporarily.

51
Q

non-competitive inhibition

A

the inhibitor binds with the enzyme at a site OTHER THAN THE ACTIVE SITE, alters the shape of the enzyme and inactivates it.

Non-competitive inhibition may be reversible.

52
Q

Cofactors

A

non-protein enzyme helpers

53
Q

coenzymes

A

organic cofactors

54
Q

where may enzymes be found within the cell?

A

Grouped into complexes

Incorporated into membranes

Contained inside organelles

biology (5 decks)

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