Chapter 3 Flashcards

(60 cards)

1
Q

Organic Molecules

A

Carbon based molecules

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2
Q

Isomers

A

same formula, differently arranged atoms

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3
Q

Structural Isomers

A

differ in how atoms are joined together

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4
Q

cis-trans isomers

A

differ in orientation around a double bond

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5
Q

Optical Isomers

A

occur when C atom has 4 different groups attached to it

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6
Q

4 molecules that make up life

A

Proteins, Carbohydrates, lipids, Nucleic acids

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7
Q

Macro Molecules

A

molecules containing thousands or more atoms

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8
Q

Functional Group

A

small groups of atoms that have specific chemical properties

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9
Q

R-OH

A

Hydroxyl group

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10
Q

R-COOH

A

Carboxyl Group

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11
Q

R-NH2

A

Amino Group

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12
Q

R-PO4-2

A

Phosphate group

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13
Q

Hydroxyl Group Properties

A

Polar, forms hydrogen bonds with water to help dissolve molecules. Enables linkage to other molecules by condensation

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14
Q

Carboxyl Group Properties

A

Charged; acidic. ionizes living tissues to form COO- and H+. Enters condensation by giving up an -OH.

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15
Q

Amino Group Properties

A

Charged; basic accepts H+ in living tissues to form NH3+. Enters condensation by giving up H+

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16
Q

Phosphate Group Properties

A

Charged; acidic. Enters condensation reactions by giving up -OH. When bonded to another phosphate, hydrolysis releases a lot of energy

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17
Q

Condensation Reaction

A

Form polymers- energy required and H2O is removed

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18
Q

Hydrolysis Reaction

A

break down polymers into monomers, energy is released, H2O consumed

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19
Q

Amino acids

A

monomer of proteins, have a carboxyl and amino group and function as both an acid an a base

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20
Q

Polypeptide Chain

A

single unbranched chain of amino acids

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21
Q

Peptide Link/Bond

A

amino acids bounded covalently in a condensation reaction

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22
Q

How many protein structures are there?

A

4 ( Primary, secondary, tertiary, quaternary)

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23
Q

Primary Structure

A

Determines how a protein folds

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24
Q

Secondary Structure

A

localized areas of folding (alpha and beta pleated sheets)

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25
Tertiary Structure
folding into a 3-D shape of one polypeptide
26
Quaternary Structure
Two or more folded proteins joining together
27
Denaturing Proteins
protein whose secondary and tertiary structure has been broken down
28
What denatures a protein?
temperature, pH, High Concentration of polar molecules, non-polar substances
29
Chaperones
3-D structures that protect proteins and prevent bad reactions
30
Carbohydrate Formula
CH2O
31
Monosaccharides
simple sugars
32
Disaccharides
two simple sugars link by covalent bonds
33
Oligosaccharides
3-20 monosaccharides
34
polysaccharides
large polymer of monosaccharides, can contains hundreds or thousands of monosaccharides
35
Why are carbs important?
source of stored energy, transport energy, carbon skeleton of other molecules, form extracellular structures
36
Glyceraldehyde
three carbon, smallest monosaccharide, only exists as a straight chain
37
Pentoses
five carbon monosaccharides
38
Hexoses
six carbon monosaccharides
39
Glucose
monosaccharides, used by all cells as an energy source
40
Glycosidic Linkage
covalent bond formed from a condensation reaction that joins monosaccharides
41
Lipid
Nonpolar hydrocarbons, insoluble in water
42
Fats + oils
store energy
43
Phospholipids
structural role in cell membrane, fatty acid bound to glycerol, a phosphate group replaces one fatty acids
44
carotenoids + chlorophylls
capture light energy in plants
45
steroids + modified fatty acids
Hormones and vitamins
46
animal fat
thermal insulation
47
nerve coating
electrical insulation
48
oil + wax
repel water on skin, fur, and feathers
49
Fatty acid
nonpolar hydrocarbon chain with polar hydroxyl group
50
triglycerides
three fatty acids + glycerol
50
Saturated fatty acid
no double bond between carbons
51
Unsaturated fatty acids
one or more double bonds in the carbon chain
52
Ampithatic
2 opposing chemical properties in one molecule
53
Bilayer
The lining up of phospholipids in water so that the hydrophobic tails face inward and the phosphate heads face outwards
54
Acid
When dissolved in water, they release hydrogen ions
55
Base
Accept hydrogen ions
56
Weak acid
Not all acid molecules dissociate into ions
57
Weak base
does not fully accept all hydrogen ions
58
Buffer
weak acid and its corresponding base, useful for maintaining pH in the body, decreases the acidifying effect of an added acid
59
Law of mass action
addition of a reactant on one side of a reversible system drives the system in the direction that uses up that compound