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Biology 12 > Biochemistry > Flashcards

Biochemistry Flashcards

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1
Q

Atomic Number

A

the number of protons and electrons

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2
Q

Atomic Mass

A

weight of protons and neutrons

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3
Q

Oxidization Number

A

the number of bonds valence shell will make

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4
Q

Electronegativity

A

atom’s ability to attract electron in bond

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5
Q

Ionic Bonding

A

Intramolecular force - transfer of electrons, forms a crystal lattice

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6
Q

Covalent Bonding

A

Intermolecular force - both nuclei pull on atom, sharing of electrons - since electrons are in constant motion there are temporary dipoles

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7
Q

Polar Bonds

A

Intermolecular force - weak partial charges on molecule - due to electronegativity difference - electrons are unequally shares

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8
Q

Hydrogen Bonding

A

Strongest Intermolecular force - weak connections between partial charges

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9
Q

Hydrophilic

A

water loving, polar

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10
Q

Hydrophobic

A

afraid of water, non polar

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11
Q

Acid

A

high concentration of H+ ions, proton donor (pH less than 7)

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12
Q

Base

A

high concentration of OH- ions, proton acceptor (pH greater than 7)

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13
Q

Buffers

A
  • acts as a proton donor as solution becomes more basic - acts as a proton acceptor as solution becomes more acidic - moderates change in pH
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14
Q

Carbonic acid

A

A common buffer - carbonic acid (basic) when solution is more acidic - H+ and bicarbonate (acidic) when solution is more basic

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15
Q

Special Properties of Water

A
  1. Solvent (medium for chemical reactions)
  2. Adhesion (for non polar) / Cohesion (for polar)
  3. Less dense at 0 than at
  4. less dense as solid 4. High Specific Heat
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16
Q

Mole

A

unit of amount of substance

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17
Q

Molar Mass

A

mass of given substance/mol

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18
Q

Molarity

A

mol/L…molar concentration

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19
Q

Hypertonic

A

solution with a higher concentration of solute

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20
Q

Isotonic

A

maintained balance solution

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21
Q

Hypotonic

A

solution with a lower concentration of solute

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22
Q

Condensation synthesis

A

is a chemical reaction in which two molecules or moieties, often functional groups, combine to form a larger molecule, together with the loss of a small molecule. (forms water with OH and H from each molecule)

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23
Q

Hydrolysis

A

reaction that breaks down polymers

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24
Q

Skeletal formula

A

representation of molecules bonding and geometry

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25
Q

Structural formula

A

shows how atoms of molecule are chemically bonded

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26
Q

Molecular formula

A

shows number of each type of atom in the compound

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27
Q
A

Name: Hydroxyl

Shortform: OH

Molecule Type: Alcohol

Ending: -ol

Properties/Polarity: polar and soluble

Found in: carbohydrates, lipids, proteins, and nucleic acids

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28
Q
A

Name: Carboxyl

Shortform: COOH or HOOC

Molecule Type: Organic Acid

Ending: -ic acid, -ate

Properties/Polarity: weakly ionic, acidic, soluble

Found in: proteins and lipids

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29
Q
A

Name: Ketone Carbonyl

Shortform: CO

Molecule Type: Ketone

Ending: -one

Properties/Polarity: weakly polar, somewhat soluble, strong smelling

Found in: carbohydrates and nucleic acids

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30
Q
A

Name: Aldehyde Carbonyl

Shortform: CHO

Molecule Type: Aldehyde

Ending: -al

Properties/Polarity: weakly polar, somewhat soluble, strong smelling

Found in: carbohydrates and nucleic acids

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31
Q
A

Name: Amino

Shortform: NH2 or NH or N

Molecule Type: amine, secondary amine, tertiary amine

Ending: -ine

Properties/Polarity: basic, soluble

Found in: proteins and nucleic acids

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32
Q
A

Name: Sulfhydryl

Shortform: SH

Molecule Type: thiol

Ending: thio

Properties/Polarity: non polar, not soluble, smelly

Found in: proteins

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33
Q
A

Name: Phosphate

Shortform: P

Molecule Type: phosphate

Ending: phospho

Properties/Polarity: strongly ionic, very soluble, acidic

Found in: nucleic acids

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34
Q

monomer

A

simple unit molecules from which lareger molecules are built

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35
Q

dimer

A

2 monomers covalently bonded

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36
Q

polymer

A

many molecules/units

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37
Q

oligiomer

A

3-20 monomer chain

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38
Q

What makes polymers?

A

Carbohydrates, Proteins and Nucleic Acids. Lipids do not make polymers but instead glycerides, because they are non polar.

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39
Q

Carbohydrates

A
  • made up of CHO in a 1:2:1 ratio
  • energy storage molecule (short term)
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40
Q

Monosaccharides

A
  • single sugar, relativley small to transport things
  • small structure is more soluble as long as there is polarity
  • only functional group present is OH
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41
Q

Sterioisomer

A

have same molecular formula and sequence of bonds, different 3D

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42
Q

Structural Isomer

A

same chemical formula, different structure

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43
Q

Glucose

A

aldose

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44
Q

Fructose

A

ketose

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45
Q

Alpha isomer

A

when hydroxyl on C#1 faces down

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46
Q

Beta isomer

A

when hydroxyl on C#1 faces up

47
Q

Disaccharides

A
  • 2 sugars
  • store twice as much energy / moleculer
  • less osmotic pressure because concentration is reduced by 1/2, pass through membrane easier
  • exisits in alpha isomers
48
Q

Examples of Disaccharides

A

Maltose (glucose+glucose)

Sucrose (glucose+fructose)

Lactose (glucose+galactose)

49
Q

Polysaccharides

A
  • less water can react with chain making it more insoluble
  • long term storage
50
Q

Starches

A

alpha polysaccharides

51
Q

Beta Glucose

A

forms linear chains with the OH and methyl side, can stack closer in this shape (ex. Cellulose)

52
Q

Alpha Glucose

A

Alpha Glucose forms chains of heleces held together by hydrogen bonds (ex. amylose, amylopectin, glycogen)

53
Q
A

Glycosidic Bond

54
Q

Chitin

A
  • modified form of beta glucose
  • replaces hydrocyl with more polar ‘R’ group
  • structurally strong
  • chemical reactions stronger because more polar
55
Q

Lipids

A
  • majority of structure is nonpolar and is hydrophobic
  • more energy by less mass

Results of Hydrophobic Nature

  1. Waterproofing
  2. Thermal Insulator
  3. Electrical Insulator
56
Q

Structure of Lipids

A
  • triglycerides consist of glycerol condensed with 3 fatty acids
57
Q

Fatty Acid

A

hydrocarbon chain with carboxyl on one end

58
Q
A

Ester bond: formed when hydroxyl on glycerl condense with cabroxyls

(bond between glycerol and carboxyl)

59
Q

Saturated

A

all single bonds (solid state- ex. butter)

60
Q

Unsaturated

A

double bonds (liquid state- ex. oil)

61
Q

Monounsaturated

A

1 double bond

62
Q

Polyunsaturated

A

2 or more double bonds

63
Q

Oleic Acid

A

most abundant fatty acid on olive oil, kinked shape, less dense

64
Q

Hydrogenation

A

adding hydrogens to break double bonds

65
Q

Phospholipids

A
  • modified triglyceride by replacing fatty acid with phosphate, Na or K
  • polar funcitonal group on top
  • amphiphilic
66
Q

Amphiphilic

A

one end hydrophobic one end hydrophilic

67
Q

Waxes

A
  • complex organic ester
  • long chain hydroxyl +fatty acid (OH on end )
68
Q

Steroids

A
  • communication molecule
  • non polar, derived from cholosterol
69
Q

Membranes

A
  • slectively permeable membrane made by phospholipids
  • amphiphilic nature allows it to form bilayers
  • polar face out, non polar face in
70
Q

Fluid Mosaic Model

A

-membranes are composed of a Phospholipid Bilayer with various protein molecules floating around within it. The ‘Fluid’ part represents how some parts of the membrane can move around freely, if they are not attached to other parts of the cell.

71
Q

Phospholipids (membranes)

A
  • impermeable to large soluble and polar molecules
72
Q

Transmembrane Proteins

A

(carriers, channels, and receptors)

  • transmission of information into cell
73
Q

Interior Proteins

A
  • determine shape of cells as well as acting as anchor site
74
Q

Glycoproteins

A
  • self recognition, major histocompatibility complex, made with oligiosaccharides
75
Q

Glycolipids

A
  • tissue recognition, made with oligiosaccharides
76
Q

Cholesterol

A
  • membrane fluidity, increase in cholesterol decreases membrane fluidity
77
Q

Types of membrane transport

A
  1. Passive transport - does not require energy
  2. Active transport - requires energy
78
Q

Types of passive transport

A
  1. Passive diffusion
  2. Facilitated diffusion
  3. Osmosis
79
Q

Passive diffusion

A
  • natural process for nonpolar molecules pass across membrane
  • net movement from an area of high concentration to low concentration
  • based on random and molecular motion of particles
80
Q

Facilitated diffusion

A
  • a protein facilitates/helps atom get through channel
  • Carrier or channel proteins
  • larger or polar molecules use this
  • net movement from an area of high concentration to low concentration
81
Q

Osmosis

A
  • low concentration and high water potential (pressure)
  • movement of water from hypotonic solution into a cell
82
Q

Types of active transport

A
  1. protein carrier
  2. endocytosis
  3. exocytosis
83
Q

Protein carrier

A
  • transfer of molecules against concentration gradient
  • requires energy from ATP
84
Q

Endocytosis

A

Particles being engulfed into membrane

85
Q

Exocytosis

A

Particles being released by membrane

86
Q

Peptides and proteins

A
  • contain amino and carboxyl group
  • R group made of CHNOS
87
Q

Monomer of protein (amino acid)

A

Peptide

88
Q

Polymer of amino acid

A

Polypeptide chains

89
Q

R Differ in

A
  • size
  • shape
  • polarity
  • ionization (acidic and basic)
  • special editions (funcitonal groups, sulfur)
90
Q

Primary structure

A
  • sequence of amino acids, determined by DNA
91
Q

Secondary structure

A
  • involve the bond angles that are produced by particular sequences of amino acids
  • twisting of the chain due to R-groups and C=O and NH groups
  • alpha helix and beta pleated sheet held together by hydrogen bonds
92
Q

Tertiary folding

A
  • the globule folding of the molecule as a result of attractions and repulsion between different parts of the chain based on electrical charges, attraction to water, size and shape restrictions
93
Q

Structures 1-4

A

1-3 found in all peptides

94
Q

Quaternary structure

A
  • the folding together of multiple chains to produce a more complex protein
95
Q

Nucleic acids

A
  • Carrie coded information about primary structure
  • linear polymers
96
Q

Monomers in nucleic acid

A

nucleotide

97
Q

What is a nucleotide made of?

A
  • a phosphate group, pentose monosaccharide, and a purine or pyrimidine nitrogen base
98
Q

Purine

A
  • double ring structure
  • adenine and guanine
99
Q

Pyrimidine

A
  • single ring structure
  • cytosine, thymine and uracil
100
Q

RNA

A
  • ribose sugar (OH at C#2)
  • adenine, guanine, cytosine, and uracil
  • single-stranded polymer
101
Q

DNA

A
  • deoxyribose sugar (H at C#2)
  • adenine, guanine, cytosine, and thymine
  • double-stranded polymer
102
Q
A

Peptide bond

103
Q

Bonding of 2 nucleotides happens between C#__ and C#__

A

Bonding of 2 nucleotides happens between C#3 and C#5

104
Q

What types of purine and pyrimidine match up?

A

AT GC

AU GC

105
Q
A

Phosphodiester linkage

106
Q

What are enzymes?

A
  • Proteins that act as catalysts within living cells
  • Can facilitate same chemical reactions over and over again
  • Lower activation energy
107
Q

What are enzymes made of?

A

composed of one or more long chains of interconnected amino acids (polypeptides)

108
Q

What are the two models of enzyme action?

A

Lock and Key

The substrate simply fits into the active site to form a reaction intermediate.

Induced Fit

when the active site on the enzymes makes contact with the proper substrate, the enzyme molds itself to the shape of the molecule

109
Q

What variables can affect enzyme action (rate of reaction)?/ What is the effect of each variable?

A
  1. pH (H+ and OH- ions)
    - When you change pH to more acidic greater concentration of H+ ions there would be ionic bonds with the amino or change O to carboxyl group, will repel the amino acid and bonds the folded enzyme will unravel, changing the shape so the substrate will not fit in it.
    - optimum point is balance of OH- and H+ that allow enzyme to remain/ maintain perfect shape, stabilize

more acidic then more unfolded called denaturing

more basic then more unfolding denaturing

  • OH- will attract amino group but does not attract O+ so no carboxyl, depends on how many OH, concentration dependent
    2. Temperature
  • As temp increases the rate of reaction increases because more frequent collisions
  • enzyme has flexibility to bond that is more rigid at low temp and very high at high temp
  • at optimal temp range, there is the most collisions being able to reduce fit without compromising the shape
  • the rate goes down afterwards because you can break H bonds (which hold up tertiary structure) and the enzyme will unfold
    3. Concentration of substrates
  • at a certain point the speed in which a reaction occurs the rate does not change
  • if you have more substrates than enzymes, the number of bonds is limited, called saturation

Concentration of enzyme

  • More enzymes more probability of binding

Salt concentration (same as why pH affects)

  • Salt is ionic compound so one +ve and –ve ion
110
Q

Regulation (promote or inhibit certain chemical reactions)

Explain one way that an enzyme can be regulated.

A
  • An inhibitor may bind to an enzyme and block binding of the substrate, for example, by attaching to the active site. This is called competitive inhibition, because the inhibitor “competes” with the substrate for the enzyme.
  • In noncompetitive inhibition, the inhibitor doesn’t block the substrate from binding to the active site. Instead, it attaches at another site and blocks the enzyme from doing its job. This inhibition is said to be “noncompetitive” because the inhibitor and substrate can both be bound at the same time.
  • Cooperativity: the substrate itself can serve as an allosteric activator (bind to locations on an enzyme other than the active site, causing an increase in the function of the active site): when it binds to one active site, the activity of the other active sites goes up.
  • Feedback inhibition works by deactivating an enzyme using the product of the reaction the enzyme catalyzes. Enzymes bind to molecules with active sites that are specifically designed to fit with the molecule undergoing the reaction. These enzymes have a second active site for the reaction product to bind to. This causes the enzyme to spatially re-arrange so it can no longer bind to the initial reagent and the reaction stops. Many mechanisms, such as bile acid synthesis in the liver and cellular respiration, use feedback inhibition on a regular basis.
  • A zymogen requires a biochemical change (such as a hydrolysis reaction revealing the active site, or changing the configuration to reveal the active site) for it to become an active enzyme (converted into an enzyme when activated by another enzyme). … Enzymes like pepsin are created in the form of pepsinogen, an inactive zymogen.
111
Q

Explain the reasons why carbon is an ideal element for life


A
  • forms 4 bonds
  • a large variety
  • large stable molecules can form because of a decreased potential energy
  • low energy levels, greater ENC
  • small input of energy to break the bonds
112
Q

Compare lipids and carbohydrates as energy sources


A
  • lipids more energy/mass, more long term storage
  • carbs more short term storage
113
Q

Compare and contrast passive and active membrane transport


A
  • both allow cell to maintian homeostasis
  • both use ion channels to move ions across
  • active requires energy, passive doesn’t
  • passive moves molecules with concentration gradient, active moves against concentration gradient
114
Q

Explain how cells transport bulk materials across the cell membrane.

A

endo anc exocytosis

Biology 12 (5 decks)

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