Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

BIO 202 > Macromolecules > Flashcards

Macromolecules Flashcards

1
Q

4 Types of Macromolecules

A

1) Carbohydrates
2) Lipids
3) Nucleic Acids
4) Proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Macromolecule

A

A giant molecule formed by the joining of smaller molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Polymer

A

A long molecule consisting of many similar or identical monomers linked together by covalent bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Monomer

A

The subunit that serves as the building block of a polymer

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Condensation Reaction

A

AKA Dehydration Synthesis

Reaction that connects a monomer to another monomer or polymer

(2 molecules are covalently bonded with the loss of a water molecule)

–> One molecule donates an H+ and the other donates an OH-

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Hydrolysis

A

Reaction that breaks bonds between 2 molecules through the addition of water

(“breaking with water”)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Carbohydrates

A

Sugars: Whether that is one or a chain of them

–> Have functions in both energy and structural component of cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Monosaccharides

A

AKA Simple Sugars

The monomers of complex carbs

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Polysaccharides

A

The macromolecule of carbohydrates: Complex sugars

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Glycosidic Linkage

A

Covalent bond formed between 2 monosaccharides by a dehydration synthesis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Polysaccharides Uses

A

1) Energy storage (Ex: starch, glycogen)

2) Structural support (Ex: cellulose, glycoproteins/lipids, chitin)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Carbohydrate Molecular Structure

A

(C)n (H2O)m –> n: (2:1)m

1) If n = m –> MONO-sugar
2) If n =/ m –> POLY-sugar

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Lipids

A

Any group of large biological molecules that mix poorly, if at all, with water

Includes: fats, phospholipids, steroids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Fatty Acid

A

Monomer of Lipids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Fatty Acid Structure

A

A carboxylic acid (-COOH) with a long carbon chain

(they vary in length of chain and #/location of double bonds)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Regions of Fatty Acid

A

Hydrophobic (fatty) region = The non polar part (carbon chain)

Hydrophilic (acid) region = The polar part (COOH group –> Carboxyl end)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Fat

A

AKA Triglycerides (containing 3 glycerides)

A lipid consisting of 3 fatty acid chains linked to one glycerol molecule

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Glycerol

A

3 carbon chain: Each carbon has an OH group attached

–> This is where fatty acid chains attach through dehydration synthesis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Ester Linkage

A

The bond that connects a fatty acid to a glycerol molecule –> (More specifically attaches to one of the glycerides (3) in the glycerol)

–> Attachment through -COOH from FA and -OH from Glyc. (ionize to release water)

POLAR Bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Polarity of Fats

A

NON POLAR

–> Even though the ester linkage region is polar, the majority of the molecule is non-polar due to the long fatty acid chains

= Gives overall molecule non-polar properties

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Phospholipids

A

A glycerol with TWO fatty acid chains and a phosphate group attached (instead of the third fatty acid chain of a fat)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Unsaturated

A

Fatty acid chain contains an amount of double bonds

–> Doesn’t allow for as close packing of molecules due to the “kinks”

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Saturated

A

Fatty acid chain has ONLY single bonds

–> Allows for close packing of molecules as there are no kinks: stack together well

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Phospholipid Structure

A

Hydrophilic HEAD (where the phosphate is)

Hydrophobic TAIL (where the fatty acids are)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

Phospholipid Membranes

A

1) Phospholipid Bilayer
2) Phospholipid Micelle

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

Phospholipid Bilayer

A

Found in life –> In an aqueous environment, phospholipids align themselves in a bilayer (two layers)

–> Hydrophobic TAILS face in towards each other (don’t touch the water)

–> Hydrophilic HEADS face outwards (towards the water)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

Phospholipid Micelle

A

Only produced in labs

–> Phospholipids form a circle with tails facing in and heads facing out

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

Steroids

A

AKA Sterols

Lipids characterized by a carbon skeleton consisting of FOUR fused rings

–> Different steroids are characterized by differences in che. groups attached to the main rings

–> Precursors to steroid hormones

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

Cholesterol

A

BULKY Molecule: A sterol

–> Found in plasma membrane
–> Contributes to membrane fluidity/rigidity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

Nucleic Acids

A

A polymer consisting of many nucleotide monomers

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

Nitrogenous Bases

A

A building block of nucleotides: we got 5 of them

1) Adenine (A)
2) Guanine (G)
3) Thymine (T) — DNA
4) Cytosine (C)
5) Uracil (U) — RNA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

Purines

A

TWO Ring Bases

–> Adenine and Guanine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

Pyrimidines

A

ONE Ring Bases

–> Cytosine, Thymine, Uracil

–> Think opposite:
pyrimidine is bigger word = smaller amount of rings

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

NucleoSIDE

A

Base + Sugar –> Make up nucleoTIDES

–> Portion of a nucleotide without any phosphate group

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

DNA Nucleosides

A

1) Deoxyadenosine
2) Deoxyguanosine
3) Deoxythymidine
4) Deoxycytidine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

RNA Nucleosides

A

1) Adenosine
2) Guanosine
3) Cytidine
4) Uridine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

Ribose

A

RNA sugar (5 carbon sugar)

–> Has a hydroxyl group (-OH) on carbon 2’ (“oxygenated”)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

Deoxyribose

A

DNA Sugar (5 Carbon sugar)

–> Has ONLY a hydrogen atom on carbon 2’ (“Deoxygenated”)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

Nucleoside Structure

A

5C Sugar + Nitrogenous Base

–> Base attaches to the 1’ Carbon (“right corner”)

40
Q

NucleoTIDE

A

Monomers of a nucleic acid

–> Consists of 5C sugar, nitrogenous base, and phosphate group (1-3 of them)

= NucleoSIDE + phosphate group (1-3 of them) –> {Phosphate ester of a nucleoside}

41
Q

Nucleotide Structure

A

5C Sugar + Phosphate Group/s + Base

–> Base attaches at the 1’ Carbon (“right”)

–> Phosphate group/s attach at the 5’ Carbon (“the one sticking out on the left”)

42
Q

Precursor to DNA

A

dATP: deoxy-adenosine triphosphate

43
Q

NucleoTIDE Functions

A

1) Energy Carriers (ATP/GTP)
2) Signalling (cAMP)
3) Subunits of DNA/RNA

44
Q

DNA vs RNA

A

DNA = deoxyribonucleic acid
–> Double stranded

RNA= ribonucleic acid
–> Single stranded

45
Q

Phosphodiester Linkage

A

The link between nucleotides to create a chain

–> Dehydration reaction

–> Phosphate grp. off of 5’C of one nucleotide connects with hydroxyl grp. off of 3’C of another nucleotide = H2O

46
Q

Polar Nature of DNA and RNA

A

They are polar, in that they have two PHYSICAL POLES (not polarity with electronegativity)

–> 5’ End and 3’ End

47
Q

5’ END

A

End with a free phosphate group of a DNA/RNA chain

48
Q

3’ END

A

End with a free hydroxyl group of a DNA/RNA chain

49
Q

Base Pairing

A

Bases from two strands (that are complementary) link together through hydrogen bonding

50
Q

THE Base Pairs

A

A—T : 2 H-Bonds (weaker)

(In RNA A—U instead)

G—C : 3 H-Bonds (Stronger)

50
Q

Anti-Parallel

A

DNA strands run in opposing directions so that a 5’ end is directly next to a 3’ end

51
Q

Shape of DNA

A

Double Helix

–> Sugar backbone on outside
–> Bases/info on the inside

52
Q

Complementary

A

Each strand predicts the other strand (based off of the base pairs) –> the strands are like inverses of each other

53
Q

Base Pairing Uses

A

1) Preserve info (during DNA replication)
2) Repair Mistakes (during DNA replication)
3) Transfer info (transcribe/translate)

54
Q

Nucleic Acids Functions

A

1) Storage of genetic info
2) Transfer of genetic info (mRNA/tRNA)
3) Structural (rRNA)
4) Enzymatic Activity (ribozymes)
5) Regulation of Gene Expression (miRNA/siRNA)

55
Q

Proteins

A

Macromolecules that carry out many key cellular functions

–> Make up more than 50% of all dry mass of most cells

56
Q

Protein Functions (8)

A

1) Structural Support
2) Storage
3) Transport
4) Hormones
5) Receptors
6) Contraction
7) Defense
8) Enzymes

57
Q

Amino Acids

A

The monomers of proteins (end in -ine)

–> 20 AAs make up all the proteins in humans (all only differ in their side chains)

58
Q

Amino Acid Structure

A

Components:
1) Central (alpha) Carbon
2) Amino Group (H2N)
3) Free Hydrogen Atom
4) Carboxyl Group (COOH)
5) SIDE CHAIN –> R group (unique for each AA)

–> Amino Group = Amino End (BASIC)
–> Carboxyl Group = Carboxyl End (ACIDIC)

59
Q

Dual Properties of AAs

A

Contain both an acidic and basic end (amino vs carboxyl) ends

–> Have properties of both acids and bases

60
Q

Side Chain Classification

A

Each AA differs in their side chain

Categorization:
1) Non-Polar
2) Polar
a. Uncharge
b. Charged –> Basic (+) or Acidic (-)

–> Allows us to predict properties of a protein by knowing the majority of its AAs

61
Q

Non-Polar Side Chain

A

AA with non-polar side chain = Typically hydrophobic AA

62
Q

Polar Side Chain

A

AA with polar side chain = usually hydrophilic AA

–> Breaks into two categories:
1) Uncharged
2) Charged

63
Q

Charged Polar Side Chain

A

Breaks into two groups;

1) Basic (+ charge)
2) Acidic (– charge)

64
Q

Protein Synthesis General Sequence

A

DNA –> RNA –> Protein

–> For viruses this is a bit different (RNA –> DNA –> RNA –> Protein)

65
Q

Types of RNA for Protein Synthesis

A

1) mRNA
2) tRNA
3) rRNA

66
Q

mRNA

A

Messenger RNA: The carrier of info

–> Carries out transcription
–> Gets info from inside nucleus to outside in cytoplasm where protein synthesis occurs

67
Q

tRNA

A

Transfer RNA: The translator

–> Carries out translation
–> Translates from RNA language to AA language

–> Has CLOVERLEAF SHAPE

68
Q

rRNA

A

Ribosomal RNA: The ribosome

–> Makes up ribosomes

69
Q

Transcription

A
70
Q

Protein Synthesis Full Sequence

A

1) Transcription (DNA to RNA)
2) Translation (RNA to AA)
3) Protein Folding (AA to protein)

71
Q

Transcription

A

The process of copying a segment of DNA into RNA (mRNA specifically)

–> Purpose is to get genetic info out of nucleus for protein synthesis to occur

NOTE: This is where Thymine is replaced with URACIL

72
Q

Translation

A

The process of converting the sequence of mRNA to a sequence of Amino Acids

–> Occurs in ribosomes with aid from tRNA

73
Q

tRNA Structural Function

A

Cloverleaf Shape –> Is an “Adaptor molecule”

Has an “Acceptor” = Where the amino acid is attached

–> Essentially, is the molecule that carries AAs to where they need to be to match with the mRNA sequence

74
Q

Codon

A

3 nucleotide set –> how the genetic code is read in translation

–> Each codon ENCODES for an amino acid

75
Q

Anti-Codon

A

Complementary to mRNA: Base pairs with the codon that encodes for the specific AA being carried by tRNA

76
Q

Degenerate Genetic Code

A

Several codons encode for the same amino acid

Purpose = Mutation protection

77
Q

Silent Mutations

A

Mutation in a nucleotide that never physically manifests as the codon still codes for the same AA

(thanks to degenerate code)

78
Q

Open Reading Frame

A

(ORF) The span of genetic code between START and STOP codons

–> “Open” because the frame remains “open” for a long stretch of time (doesn’t stop and start quickly)

79
Q

Peptide Bond

A

Connects amino acids together (covalent bond)

–> COOH of one AA gets rid of its OH group and bonds to N2H of another AA with gets rid of an H atom

= H2O and peptide bond (C–N)

80
Q

Components of Polypeptide Chain

A

1) Polypeptide Backbone (repetitive)
2) Side Chains (the R groups coming off of each AA)

81
Q

Ends of Polypeptide

A

N-Terminus = Free amino group end

C-Terminus = Free carboxyl group end

82
Q

N-Terminus

A

AMINO END

–> Corresponds to 5’ end of gene

83
Q

C-Terminus

A

CARBOXYL END

–> Corresponds to 3’ end of gene

84
Q

Protein Structure

A

Determines how the protein works/its functions

–> 4 levels of structure

85
Q

Primary Structure

A

The amino acid sequence of a protein

–> Cannot be changed by environmental factors: only che. reactions or mutations

86
Q

Secondary Structure

A

The initial folding of a protein: Regions of repetitive coiling or folding of the POLYPEPTIDE BACKBONE

–> Due to H-Bonding of N and O in backbone

87
Q

Secondary Structure Possibilities

A

1) Alpha Helix
2) Beta Sheets
3) Random Coiling

88
Q

Alpha Helix

A

A protein COIL

–> H-Bonds every FOURTH peptide bond

89
Q

Beta Sheet

A

A protein sheet folded in on itself so that 2 regions are parallel

–> Strong structures

90
Q

Random Coiling

A

If protein doesn’t have alpha helix or beta sheet folding

91
Q

Tertiary Structure

A

Provides a 3D shape due to interactions between SIDE CHAINS of the AAs

–> Provides OVERALL SHAPE to the protein

92
Q

Quarternary Structure

A

Formed by interactions between separate protein chains to form a more complex molecule

–> Contains subunits: Composing proteins that create the functional unit

–> Most proteins don’t have a 4th level structure

93
Q

Determining Factors of Protein Structure

A

1) Amino Acid Sequence
2) Salt Concentration
3) pH
4) Presence of active chemicals/detergents
5) Temperature

94
Q

Denature

A

The destruction of the 2nd, 3rd, and 4th level structures causing the protein to unfold

–> Affects its function/ability

95
Q

Native Form vs Denatured Form

A

Native Form = Correct Structure

Denatured Form = Altered Structure (unfolded)

BIO 202 (33 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions