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biology quarter2 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Types of biomolecules

A

Carbohydrates
- monosaccharides (glucose and fructose)
- disaccharides (maltose, lactose and sucrose)
- Polysaccharides (starch and cellulose)
Amino Acids and Proteins
Triglycerides
Steroids

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2
Q

Substances in food

A

Digestible carbohydrates (source of our energy)
Protein
Triglycerides

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3
Q

what is carbohydrates

A

a general name for sugars, starches and cellulose
also called saccharides

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4
Q

what is the most common monosaccharides

A

glucose
fructose
galactose

isomers with the formula C6H1206

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5
Q

are polysaccharides (polymers) composed of long chains of glucose molecules (monomers) linked together by alpha linkage

A

starches

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6
Q

—— are large molecules composed of simpler repeating unites called ——

A
  • polymers
  • monomers
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7
Q

a polysaccharide composed of long chains of glucose molecules linked together by beta linkages

A

cellulose

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8
Q

with long straight chains of glucose molecules (plant starch)

A

amylose

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9
Q

with long chains of glucose molecules with periodic chains of glucose molecules coming off as branches from the straight chains (plant starch)

A

amylopectin

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10
Q

similar to amylopectin but with generally shorter and more frequent branches

A

animal starch (glycogen)

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11
Q

are the building blocks of proteins

A

amino acids

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12
Q

how many amino acids are important for producing proteins

A

20

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13
Q

each amino acid has an amine group and a carboxylic acid group separated by a

A

carbon

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14
Q

one amino acid differs from another by a side chain connected to the

A

central carbon

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15
Q

amino group of one amino acid can react with the carboxylic group of another amino acid to form an

A

amide group

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16
Q

in proteins, amide linkage is called

A

peptide bond

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17
Q

chain of amino acids linked by peptide bonds would be called a

A

polypeptide / peptide

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18
Q

if the polypeptide has more than about 50 amino acids, we call it

A

protein

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19
Q

the sequence of amino acids in the protein

A

primary structure

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20
Q

arrangement of atoms that are close to each other in the polypeptide chain is called

A

secondary structure

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21
Q

three types of secondary structure

A

a-helix
b-sheet
irregular

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22
Q

specific overall shape of the protein is called

A

tertiary structure

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23
Q

when there is a double bond between two carbon atoms and when like groups are on different carbon atoms and the same side of the double bond, the arrangement is called

A

cis

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24
Q

when the like groups are on opposite sides of the double bond the arrangement is called

A

trans

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25
Q

natural unsaturated triglycerides have the groups attached to the double-bonded carbon atoms in the cis arrangement

A

trans fat

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26
Q

hydrogenation is

A

reversable

27
Q

nucleotide structure - 2
bases - purines

A

adenine
guanine

28
Q

nucleotide structure - 3
bases - pyrimidines

A

thymine
cytosine

29
Q

nucleotide structure - 4
bases - pyrimidines

A

Uracil

30
Q

only found in DNA

A

thymine

31
Q

In RNA, thymine is replaced by

A

URACIL

32
Q

are what makes a nucleoside a nucleotide

A

phosphate groups

33
Q

are essential for nucleotide polymerization

A

phosphate groups

34
Q

exists as a single strand polymer

A

RNA

35
Q

exists as a double stranded polymer

A

DNA

36
Q

created by hydrogen bons between nucleotides

A

DNA double strand

37
Q

always bind to complementary nucleotides

A

nucleotides

38
Q

can occur in RNA but is usually within the same strand

A

Base pairing

39
Q

DNA base pairing is

A

antiparallel

40
Q

why antiparallel DNA base pairing?

A

need to shield the genetic information

is the only conformational structure to allow double helix formation

41
Q

who first determined the double helix

A

watson and crick in 1953

42
Q

most energy favorable conformation for double stranded DNA to form

A

The double helix

43
Q

the double helix Shape and size is

A

uniform for all life

44
Q

without anti parallel base pairing this conformation

A

could not exists

45
Q

are critical for binding proteins that regulate DNA function

A

Major grooves

46
Q

Sub molecules of Amino Acids

A

amino group
R group
Caboxyl group

47
Q

what are the 2 types of R group

A

Aliphatic
aromatic

48
Q

close group
positive charge

A

aromatic group

49
Q

open group
negative charge

A

aliphatic group

50
Q

cells link amino acid monomers together by

A

dehydration reactions

51
Q

the bond between adjacent amino acids is called

A

peptide bond

52
Q

Dehydration reaction = positive + negative =

A

water molecule

53
Q

Levels of protein structure

A

PRIMARY
SECONDARY
TERTIARY
QUARTERNARY

54
Q

unique sequence of amino acids

A

primary protein structure

55
Q

includes alpha helices and beta sheets which resulted from amino acids chain coiling or folding

A

secondary protein structure

56
Q

formed and maintained by hydrophobic

A

tertiary structure

57
Q

hemoglobin

A

quarternary

58
Q

can be found in the cell membrane

A

nucleus

59
Q

nucleutides components

A

5 carbon
5 sugar
5 phospate
base

60
Q

can merge aromatic and aliphatic group

A

nucleutides

61
Q

2 oxygen + 1 hydrogen =

A

1 carbon

62
Q

5 base of nucleutides

A

Cytosine
Thymine
Uracil
Adenine
Guanine`

63
Q
A

biology (2 decks)

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