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BIO 202 > Macromolecules > Flashcards

Macromolecules Flashcards

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1
Q

4 Types of Macromolecules

A

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

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2
Q

Macromolecule

A

A giant molecule formed by the joining of smaller molecules

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3
Q

Polymer

A

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

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4
Q

Monomer

A

The subunit that serves as the building block of a polymer

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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-

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6
Q

Hydrolysis

A

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

(“breaking with water”)

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7
Q

Carbohydrates

A

Sugars: Whether that is one or a chain of them

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

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8
Q

Monosaccharides

A

AKA Simple Sugars

The monomers of complex carbs

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9
Q

Polysaccharides

A

The macromolecule of carbohydrates: Complex sugars

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10
Q

Glycosidic Linkage

A

Covalent bond formed between 2 monosaccharides by a dehydration synthesis

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11
Q

Polysaccharides Uses

A

1) Energy storage (Ex: starch, glycogen)

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

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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

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13
Q

Lipids

A

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

Includes: fats, phospholipids, steroids

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14
Q

Fatty Acid

A

Monomer of Lipids

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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)

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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)

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17
Q

Fat

A

AKA Triglycerides (containing 3 glycerides)

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

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18
Q

Glycerol

A

3 carbon chain: Each carbon has an OH group attached

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

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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

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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

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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)

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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”

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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

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24
Q

Phospholipid Structure

A

Hydrophilic HEAD (where the phosphate is)

Hydrophobic TAIL (where the fatty acids are)

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25
Phospholipid Membranes
1) Phospholipid Bilayer 2) Phospholipid Micelle
26
Phospholipid Bilayer
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)
27
Phospholipid Micelle
Only produced in labs --> Phospholipids form a circle with tails facing in and heads facing out
28
Steroids
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
29
Cholesterol
BULKY Molecule: A sterol --> Found in plasma membrane --> Contributes to membrane fluidity/rigidity
30
Nucleic Acids
A polymer consisting of many nucleotide monomers
31
Nitrogenous Bases
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
32
Purines
TWO Ring Bases --> Adenine and Guanine
33
Pyrimidines
ONE Ring Bases --> Cytosine, Thymine, Uracil --> Think opposite: pyrimidine is bigger word = smaller amount of rings
34
NucleoSIDE
Base + Sugar --> Make up nucleoTIDES --> Portion of a nucleotide without any phosphate group
35
DNA Nucleosides
1) Deoxyadenosine 2) Deoxyguanosine 3) Deoxythymidine 4) Deoxycytidine
36
RNA Nucleosides
1) Adenosine 2) Guanosine 3) Cytidine 4) Uridine
37
Ribose
RNA sugar (5 carbon sugar) --> Has a hydroxyl group (-OH) on carbon 2' ("oxygenated")
38
Deoxyribose
DNA Sugar (5 Carbon sugar) --> Has ONLY a hydrogen atom on carbon 2' ("Deoxygenated")
39
Nucleoside Structure
5C Sugar + Nitrogenous Base --> Base attaches to the 1' Carbon ("right corner")
40
NucleoTIDE
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
Nucleotide Structure
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
Precursor to DNA
dATP: deoxy-adenosine triphosphate
43
NucleoTIDE Functions
1) Energy Carriers (ATP/GTP) 2) Signalling (cAMP) 3) Subunits of DNA/RNA
44
DNA vs RNA
DNA = deoxyribonucleic acid --> Double stranded RNA= ribonucleic acid --> Single stranded
45
Phosphodiester Linkage
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
Polar Nature of DNA and RNA
They are polar, in that they have two PHYSICAL POLES (not polarity with electronegativity) --> 5' End and 3' End
47
5' END
End with a free phosphate group of a DNA/RNA chain
48
3' END
End with a free hydroxyl group of a DNA/RNA chain
49
Base Pairing
Bases from two strands (that are complementary) link together through hydrogen bonding
50
THE Base Pairs
A---T : 2 H-Bonds (weaker) (In RNA A---U instead) G---C : 3 H-Bonds (Stronger)
50
Anti-Parallel
DNA strands run in opposing directions so that a 5' end is directly next to a 3' end
51
Shape of DNA
Double Helix --> Sugar backbone on outside --> Bases/info on the inside
52
Complementary
Each strand predicts the other strand (based off of the base pairs) --> the strands are like inverses of each other
53
Base Pairing Uses
1) Preserve info (during DNA replication) 2) Repair Mistakes (during DNA replication) 3) Transfer info (transcribe/translate)
54
Nucleic Acids Functions
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
Proteins
Macromolecules that carry out many key cellular functions --> Make up more than 50% of all dry mass of most cells
56
Protein Functions (8)
1) Structural Support 2) Storage 3) Transport 4) Hormones 5) Receptors 6) Contraction 7) Defense 8) Enzymes
57
Amino Acids
The monomers of proteins (end in -ine) --> 20 AAs make up all the proteins in humans (all only differ in their side chains)
58
Amino Acid Structure
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
Dual Properties of AAs
Contain both an acidic and basic end (amino vs carboxyl) ends --> Have properties of both acids and bases
60
Side Chain Classification
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
Non-Polar Side Chain
AA with non-polar side chain = Typically hydrophobic AA
62
Polar Side Chain
AA with polar side chain = usually hydrophilic AA --> Breaks into two categories: 1) Uncharged 2) Charged
63
Charged Polar Side Chain
Breaks into two groups; 1) Basic (+ charge) 2) Acidic (-- charge)
64
Protein Synthesis General Sequence
DNA --> RNA --> Protein --> For viruses this is a bit different (RNA --> DNA --> RNA --> Protein)
65
Types of RNA for Protein Synthesis
1) mRNA 2) tRNA 3) rRNA
66
mRNA
Messenger RNA: The carrier of info --> Carries out transcription --> Gets info from inside nucleus to outside in cytoplasm where protein synthesis occurs
67
tRNA
Transfer RNA: The translator --> Carries out translation --> Translates from RNA language to AA language --> Has CLOVERLEAF SHAPE
68
rRNA
Ribosomal RNA: The ribosome --> Makes up ribosomes
69
Transcription
70
Protein Synthesis Full Sequence
1) Transcription (DNA to RNA) 2) Translation (RNA to AA) 3) Protein Folding (AA to protein)
71
Transcription
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
Translation
The process of converting the sequence of mRNA to a sequence of Amino Acids --> Occurs in ribosomes with aid from tRNA
73
tRNA Structural Function
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
Codon
3 nucleotide set --> how the genetic code is read in translation --> Each codon ENCODES for an amino acid
75
Anti-Codon
Complementary to mRNA: Base pairs with the codon that encodes for the specific AA being carried by tRNA
76
Degenerate Genetic Code
Several codons encode for the same amino acid Purpose = Mutation protection
77
Silent Mutations
Mutation in a nucleotide that never physically manifests as the codon still codes for the same AA (thanks to degenerate code)
78
Open Reading Frame
(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
Peptide Bond
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
Components of Polypeptide Chain
1) Polypeptide Backbone (repetitive) 2) Side Chains (the R groups coming off of each AA)
81
Ends of Polypeptide
N-Terminus = Free amino group end C-Terminus = Free carboxyl group end
82
N-Terminus
AMINO END --> Corresponds to 5' end of gene
83
C-Terminus
CARBOXYL END --> Corresponds to 3' end of gene
84
Protein Structure
Determines how the protein works/its functions --> 4 levels of structure
85
Primary Structure
The amino acid sequence of a protein --> Cannot be changed by environmental factors: only che. reactions or mutations
86
Secondary Structure
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
Secondary Structure Possibilities
1) Alpha Helix 2) Beta Sheets 3) Random Coiling
88
Alpha Helix
A protein COIL --> H-Bonds every FOURTH peptide bond
89
Beta Sheet
A protein sheet folded in on itself so that 2 regions are parallel --> Strong structures
90
Random Coiling
If protein doesn't have alpha helix or beta sheet folding
91
Tertiary Structure
Provides a 3D shape due to interactions between SIDE CHAINS of the AAs --> Provides OVERALL SHAPE to the protein
92
Quarternary Structure
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
Determining Factors of Protein Structure
1) Amino Acid Sequence 2) Salt Concentration 3) pH 4) Presence of active chemicals/detergents 5) Temperature
94
Denature
The destruction of the 2nd, 3rd, and 4th level structures causing the protein to unfold --> Affects its function/ability
95
Native Form vs Denatured Form
Native Form = Correct Structure Denatured Form = Altered Structure (unfolded)

BIO 202 (33 decks)

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