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Bio 110 > Chapter 3 > Flashcards

Chapter 3 Flashcards

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Biology 101 flashcards
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
Q

Tertiary Structure

A

folding into a 3-D shape of one polypeptide

26
Q

Quaternary Structure

A

Two or more folded proteins joining together

27
Q

Denaturing Proteins

A

protein whose secondary and tertiary structure has been broken down

28
Q

What denatures a protein?

A

temperature, pH, High Concentration of polar molecules, non-polar substances

29
Q

Chaperones

A

3-D structures that protect proteins and prevent bad reactions

30
Q

Carbohydrate Formula

A

CH2O

31
Q

Monosaccharides

A

simple sugars

32
Q

Disaccharides

A

two simple sugars link by covalent bonds

33
Q

Oligosaccharides

A

3-20 monosaccharides

34
Q

polysaccharides

A

large polymer of monosaccharides, can contains hundreds or thousands of monosaccharides

35
Q

Why are carbs important?

A

source of stored energy, transport energy, carbon skeleton of other molecules, form extracellular structures

36
Q

Glyceraldehyde

A

three carbon, smallest monosaccharide, only exists as a straight chain

37
Q

Pentoses

A

five carbon monosaccharides

38
Q

Hexoses

A

six carbon monosaccharides

39
Q

Glucose

A

monosaccharides, used by all cells as an energy source

40
Q

Glycosidic Linkage

A

covalent bond formed from a condensation reaction that joins monosaccharides

41
Q

Lipid

A

Nonpolar hydrocarbons, insoluble in water

42
Q

Fats + oils

A

store energy

43
Q

Phospholipids

A

structural role in cell membrane, fatty acid bound to glycerol, a phosphate group replaces one fatty acids

44
Q

carotenoids + chlorophylls

A

capture light energy in plants

45
Q

steroids + modified fatty acids

A

Hormones and vitamins

46
Q

animal fat

A

thermal insulation

47
Q

nerve coating

A

electrical insulation

48
Q

oil + wax

A

repel water on skin, fur, and feathers

49
Q

Fatty acid

A

nonpolar hydrocarbon chain with polar hydroxyl group

50
Q

triglycerides

A

three fatty acids + glycerol

50
Q

Saturated fatty acid

A

no double bond between carbons

51
Q

Unsaturated fatty acids

A

one or more double bonds in the carbon chain

52
Q

Ampithatic

A

2 opposing chemical properties in one molecule

53
Q

Bilayer

A

The lining up of phospholipids in water so that the hydrophobic tails face inward and the phosphate heads face outwards

54
Q

Acid

A

When dissolved in water, they release hydrogen ions

55
Q

Base

A

Accept hydrogen ions

56
Q

Weak acid

A

Not all acid molecules dissociate into ions

57
Q

Weak base

A

does not fully accept all hydrogen ions

58
Q

Buffer

A

weak acid and its corresponding base, useful for maintaining pH in the body, decreases the acidifying effect of an added acid

59
Q

Law of mass action

A

addition of a reactant on one side of a reversible system drives the system in the direction that uses up that compound

Bio 110 (11 decks)

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