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SBI4U- uni prep > Unit 1- biochemistry > Flashcards

Unit 1- biochemistry Flashcards

1
Q

what are the two kinds of chemical bonding?

A
  • Intramolecular: the force that holds atoms together within a molecule (super strong)- sew and needle
  • intermolecular: the force that holds the two molecules together( super weak) - velcro
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2
Q

ionic bonds

A
  • complete transfer of electrons
  • generates two oppositely charged ions
  • metal loses electrons (becomes positively charged) and non-metal gains electrons (becomes negatively charged)
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3
Q

Covalent bond

A

a bond formed between atoms with similar electronegativities- affinity or desire for electron
- they share electrons to obtain octet configuration.
- have two different subbonds

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4
Q

Non- polar covalent bonds

A
  • formed between the same atoms or ones that have VERY similar electronegativities
    Cl — Cl –> n.p
    0.5> elec negativity
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5
Q

Polar covalent

A
  • formed between atoms with slightly different elect negativity
  • 0.5< x ≤ 1.9
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6
Q

strongest type of intermolecular molecules.

A
  • dipole-dipole: occurs when partially positive interacts with partially negative of the neighboring molecule
  • in order to exist it needs partially charged ions
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7
Q

Hydrogen bonding:

A
  • a special kind of dipole to dipole
  • occurs between hydrogen atoms bonded to H, N, O,
  • the positive end of hydrogen is attracted to the charged negative end of O, F, N.
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8
Q

Condensation: aka dehydration

A

-ANABOLISM: assembly of a polymer
-as two monomers are joined together to make a polymer chain– h20 is removed

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9
Q

hydrolysis:

A
  • Catabolism: disassembly of large polymers back into monomers
  • one hydrogen is added into the hydroxyl group and the other to the other monomer
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10
Q

categories of biological molecules:

A
  • carbohydrates
  • lipids
  • proteins
  • nucleic acids
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11
Q

hydroxyl group

A

O-H

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12
Q

Carbonyl (aldehydes)

A

C=O
|
H

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13
Q

Carbonyl (ketones)

A

C=O
|
R

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14
Q

Carboxyl

A

COOH

or

O
||
C
||
OH

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15
Q

amino

A

– NH2

H
||
N
||
H

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16
Q

Phosphate group

A

PO4^2
or

+

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17
Q

Cohesion

A
  • only polar causes cohesion since it is polar
  • the ability for water to bond with itself
  • gives rise to surface tension
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18
Q

Adhesive

A
  • only polar causes adhesion because water is polar
  • the ability for water to bond to other polar or ionic substances. - meniscus and hydrophilic interactions.
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19
Q

Macromolecules

A
  • large complex organic molecules
  • ” form fits function”
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20
Q

Monomer

A

small molecules chemically joined to form larger, more complex biological molecules called polymers

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21
Q

polymers

A

long chains of monomer joined chemically.

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22
Q

metabolism

A

the breaking down and building up of metabolic processes.

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23
Q

Monosaccharide

A

single sugar molecules AKA “simple sugars”

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24
Q

isomer

A

monosaccharides that have the same chemical formula, but different shapes and arrangements.

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25
Q

Disaccharides

A
  • two monosaccharides joined together by the condensation/ dehydration reaction
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26
Q

3 examples of disaccharides

A
  • sucrose (qlucose+ fructose)
  • lactose ( glucose +galactose)
  • maltose ( glucose+ glucose)
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27
Q

3 examples of monosacrides

A

-Glucose
-fructose
- galactose

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28
Q

what is a glycosidic linkage

A

the covalent bonds formed between two monosaccharide monomers
ex- alpha glucose.

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29
Q

4 examples of polysacchrides

A
  • Starch
  • cellulose
  • glycogen
  • chitin
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30
Q

alpha form

A
  • when the ring closes, the hydroxyl group on c-1 is locked below the plane of rings
    vvvvvvv
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31
Q

beta form

A
  • when the ring closes, the hydroxyl group on c-1 is locked above the plane of rings
  • unable to break
  • ^ v ^ v- every other glucose is turned “upside down”
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32
Q

alpha form examples

A
  • startch
  • glycogen
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33
Q

quick energy sugarrs

A

disaccharides

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34
Q

fast and short term energy

A

monosaccharides

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35
Q

what are polysaccharides

A
  • complex carbohydrates
    -the polymers
  • 4 main groups
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36
Q

1st example of a polysaccharide

A
  • plant startches :
    -long branches of glucose monomers
  • storages of energy for plants
    2 types:
  • amylose: ( 1 chain of monomers)
  • amylopectin (2 chains of monomers)
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37
Q

2nd example of a polysaccharide

A
  • animal starches:
  • storage of energy in the liver and skeletal muscles.
  • highly branched chains of glucose monomers
  • glycogen (3 chains)
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38
Q

what is the polarity of alpha glucose??

A
  • alpha glucose is polar
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39
Q

what happens if polysaccharides are too big

A

water will not be able to surround them and they will not be able to be dissolved.

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40
Q

third example of a polysaccharide:

A

cellulose: AKA fiber
- found in the cell wall
- structure component
- most abundant
- undigestable due to its beta form

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41
Q

difference between alpha and beta forms:

A
  • alpha is when the bonds occur all in the carbon 6 same row below the plane and an example would be starch.
  • beta is when carbon 6 causes every other glucose to turn upside down. an example is cellulose. -
42
Q

the fourth example of polypeptide?

A
  • chitin ( insects, crabs, lobsters, shrimp)
  • a structural component
  • glucose monomers with nitrogen
  • contains side chains on c-2 instead of hydroxyl group
43
Q

what two polysaccharides are for storage? what is their glycogen linkage form? are they digestible?

A
  • starch and glycogen
  • alpha glycogenic linkage
  • can be digestible
44
Q

what two polysaccharides are for structure? what is their glycogen linkage form? are they digestible?

A
  • cellulose and chitin
  • beta glycogenic linkage
  • can not be digestible
45
Q

what are the general characteristics of lipids?

A
  • three large and diverse groups of molecules
  • lipids are not polymers
  • the lipid groups differ structurally
  • all lipids are non-polar
    and since water is polar they do not attract each other
  • they have high C-H content
46
Q

what are the three groups of lipids?

A
  • fats/ oils
  • phospholipids
  • steroids
47
Q

what do you know about the first sub- group of lipids

A
  • fats and oils
  • energy reserves for animals
  • used for insulation
  • non- polar
  • only contains oxygen ( not much), hydrogen, and carbon
  • basic structure is triglyceride
48
Q

what is the basic structure of triglyceride?

A
  • one glycerol (3 carbon alcohol)
  • three fatty acids ( long hydrocarbon chains, carboxylic acid attached on one end, always have even number of carbon atoms in the chain)
49
Q

what are two types of fats?

A
  • saturated: (solids)– full, can not hold anymore. more animal fats
    ((( no double bonds)))
  • unsaturated (liquids) – “unfull” can still hold more. more plant fats
    ((( active double bonds)))
50
Q

why are unsaturated fats liquid?

A
  • because they double bond creates angles in the carbon skeleton of the fatty acid that prevents them from packing together and solidifying at room temperature
51
Q

why do we need fats in our diet?

A
  • a source of many essential fatty acids needed for hair and skin
  • needed for phospholipids in all the membranes of the cell
  • essential for the absorption of all fat-soluble vitamins, such as vitamins A,D, E
  • also for long-term energy once the body runs out of short-term energy
52
Q

what do you know about the second sub- group of lipids?

A
  • phospholipids:
  • phospholipids have a partial exception to the hydrophobic lipid rule.
  • have both a polar and a non polar region on each molecule.
53
Q

meaning of amphilic

A

one part is water-loving, and one part hates water.

54
Q

what part of a phospholipid loves water/ soluble

A
  • hydrophilic head
  • polar “head” glycerol and phosphate group
  • because it contains a charged phosphate function group that replaces the 3rd fatty acids.
55
Q

what part of a phospholipid hates water/ insoluble

A
  • hydrophobic tail
  • two non- polar fatty acid “tails”
56
Q

what is phospholipids a major component of?

A

forms a double layer in all cell membrane

57
Q

what does the double membrane of a phospholipid looks like?

A
  • the polar heads are oriented towards the aqueous areas
  • the non-polar fatty acids form a non-polar lipid barrier between the inside and outside of the cells.
58
Q

what is the main function of phospholipids?

A

covers all cells, is the membrane of all cells

59
Q

what do you know about the third sub-group of lipids?

A
  • steroids:
  • different structure than fats and phospholipids
60
Q

what is the characteristic structure od steriods?

A
  • 4 fused rings aka (sterol backbone)
  • the steroid backbone is found in all steroid backbone
  • what attaches to the backbone determines what type of steroid it is.
61
Q

examples of steroid

A
  • cholestrol
  • sex hormones
62
Q

what are steroids used for?
give 5 examples…

A
  • sex hormones ( testosterone in males, and estrogen and progesterone in females)
  • vitamin D
  • important parts of the cell membrane
  • bile salts
  • corticosteroids from adrenals
63
Q

what is the third group of biological molecules?

A
  • proteins
64
Q

list some functions of proteins

A
  • structural proteins (skeletal and muscles)
  • enzymes
  • defense
  • hormones
  • cell movement
  • toxins
65
Q

what is the difference between tendon and ligament?

A

a tendon attaches muscles and bones while ligaments attaches bone and bone.

66
Q

what is a monomer of protein?

A

amino acids

67
Q

what is the basic structure of all amino acids

A
  • central carbons with FOUR functional groups
  • amino group
  • carboxyl group
  • hydrogen
  • and an amino acid (R)
68
Q

what does the R group determine?

A
  • idenity of amino acids
  • physical properties of amino acids( size and shape)
  • chemical properties of amino acids( polarity and [H+]
69
Q

what are the three categories of amino acids?

A
  • non- polar
  • uncharges polar
  • charged polar ( negatively- acid or positively- basic )
70
Q

what is the polymer of amino acids called?

A
  • polypeptide chain/ linear chain
71
Q

what is removed everytime two amino acids are chemically bonded?

A

molecule of water is removed.

72
Q

what is the bond that forms between the amino acids? what is it called?

A

the bond between amino acids is a covalent bond called “ peptide bond”

73
Q

how many levels of structure are in proteins? what are they?

A
  • there are four levels of protein structure”
  • primary level
  • secondary level
  • tertiary levels
  • quaternary level
74
Q

what is the primary level of a protein?

A
  • the specific sequence of amino acids that join the polypeptide chain
  • when peptide bonds form they produce a long chain with a carboxylic acid group on one end and an amino acid on the other.
75
Q

what determines the primary structure of the polypeptide chain?

A

the gene in the dna coding for the protein

76
Q

what is the secondary level of proteins?

A
  • the way the polypeptide chain is coiled up and folded UPON ITSELF.
  • there are two types of secondary structures:
77
Q

there are two types of secondary structures, what are they?

A

alpha helix: in hair and horn
- peptide chain in coiled, hydrogen bonds are between every fourth

beta pleated sheet: spider silk and silkworm
- chain is folded back with regions of chain parallel to itself
- hydrogen bonds hold it together.

78
Q

tertiary level of proteins.

A
  • the overall 3- D conformation
  • the hydrophobic “R” groups are oriented in the middle of the molecule.
  • interactions between the “R” groups of the amino acids.
79
Q

how many forces hold the tertiary conformation? what are they?

A

four forces are all intermolecular

  • hydrogen bonds
  • hydrophobic bonds
  • ionic bonding
  • disulfide bonds
80
Q

what are disulfide bonds?

A
  • are strong covalent bonds formed between two amino acids containing sulfhydryl groups in the “R” groups of amino acids
  • amino acids cysteine
81
Q

Quatenary levels of proteins.

A

-founds only in proteins composed of two or more polypeptide chain
- examples: collagen, hemoglobin,

82
Q

what is the denaturing of proteins?

A
  • the unfolding of secondary and tertiary structures.
  • not reversible, and will lose function
  • the hydrogen bonds are broken
  • if the primary structure is destroyed the whole protein is destroyed.
83
Q

three things proteins are sensitive two

A
  • high temp (fever)
  • extreme pH
  • high salt concentration
84
Q

what is the fourth group of biological molecules?

A

nucleic acids

85
Q

what is the longest polymer in the body?

A

nucleic acids.

86
Q

what is the monomer of nucleic acids?

A

nucleotide

87
Q

what is the basic structure of a nucleotide?

A
  • a 5- carbons sugar
  • phosphate group
  • nitrogen base
88
Q

what are the two types of nitrogen bases? how are they different? and list examples…

A
  • purine: double rings
    (adenine, guanine)
  • pyrimidines: single rings
    (thymine, cytosine, uracil)
89
Q

what type of base is found in all nucleic acids? DNA? and RNA?

A
  • all nucleic acids: A, G, C
  • DNA: T
  • RNA: U
90
Q

what sugar is DNA, RNA?

A

DNA: deoxyribose( missing hydroxyl group on C2)
RNA: ribose

91
Q

what happens during the condensation of amino acids?
what is it called?

A
  • the two nucleotides are joined together by a phosphate group of one nucleotide and the sugar on the other nucleotide.
  • called the “sugar-phosphate” backbone
92
Q

what is an active site?

A

the binding site for the substrate

93
Q

what is a substrate?

A
  • any molecule that is recognized by an enzyme.
  • substrate must have a similar shape
94
Q

induced fit model

A
  • describes how an enzyme changes shape to better accommodate a substrate
95
Q

activation energy:

A

the energy required to start a reaction

96
Q

what do enzymes do to the activation energy,

A

they lower it to make it more readily

97
Q

what are co enzymes-

A

an organic molecule that acts as a co-factor
organic meaning contains carbon

98
Q

cofactor-

A

a non-protein atom or molecule that binds to an enzyme and is essential for catalytic activity
- examples of cofactors: are iron, magnesium, potassium, and zinc.

99
Q

enzyme inhibitors-

A
99
Q

enzyme inhibitors-

A

SBI4U- uni prep (2 decks)

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