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AP Biology Barron > Organic Compounds > Flashcards

Organic Compounds Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

iosmers

A

org. compounds w/ same mol. formula, but different structures which cause them to have different prop.

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2
Q

types of isomers

A

structural isomers, cis-trans isomers. enantiomers

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3
Q

structural isomers

A

differ in arrangement of atoms

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4
Q

cis-trans isomers

A

differ in spatial arrangement around double bonds (not flexible like single bonds)

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5
Q

enantiomers

A

molecules that are mirror images of each other, (left handed L- and right handed D-)

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6
Q

L- vs D- fact

A

mirror images may not be equally effective, L- dopa is useful for treatment of Parkinson’s but D- dopa is not biologically active

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7
Q

Q: amino acids in cells are left or right handed?

A

all amino acids are left handed.

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8
Q

org. compounds

A

all living organisms have them, contain carbon

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9
Q

four classes of organic compounds

A

carbohydrates, lipids, proteins and nucleic acids

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10
Q

Carbohydrates

A

body uses as fuel and building materials

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11
Q

carbs constituent elements

A

C, H, O

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12
Q

ratio of H to O in all carbs

A

2:1

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13
Q

carbs == QUICK energy

A

1 gram of any carb == 4 calories when burned with a calorimeter

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14
Q

3 classes of carbohydrates

A

monosaccharides, disaccharides, and polysaccharides

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15
Q

monosaccharides

A

Chemical formula: C6H12O6, ex: glucose, galactose, and fructose, all isomers

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16
Q

conventional numbering of C in rings

A

numbering begins to the right of O

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17
Q

disaccharide

A

chemical formula: C12H22O11, two monosacc. together with a release of 1 H20

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18
Q

dehydration synthesis or condensation

A

process of joining two molecules by releasing a H20

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19
Q

glucose + glucose

A

maltose + water

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20
Q

glucose + galactose

A

lactose + water

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21
Q

glucose + fructose

A

sucrose + water

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22
Q

hydrolysis

A

break down of a compound by adding water, reverse of condensation synthesis

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23
Q

Q: sucrose + water –> glucose + fructose is an example of what?

A

hydrolysis

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24
Q

monosaccharide + monosaccharide –>

A

disaccharide + h20

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25
Q

polysaccharides

A

macromolecules, polymers of carbohydrates, formed by many monosaccharides joined together by dehydration

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26
Q

Q: What process enables monosaccharides to join together to form polysaccharides?

A

dehydration

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27
Q

Q: What are the structural polysaccs found in plants and animals?

A

cellulose (plant cell walls) and chitin (exoskeleton in arthropods and cell walls in fungi)

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28
Q

Q: What are the structural polysaccs found in plants and animals?

A

starch (forms are amylose and amylopectin) and glycogen (animal starch stored in liver and skeletal muscle)

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29
Q

4 things that are included under lipids

A

fats, oils, waxes, and steroids

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30
Q

structural components of most lipids

A

1 glycerol and 3 fatty acids

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31
Q

fatty acid

A

hydrocarbon chain with a carboxyl group at one end

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32
Q

2 varieties fatty acids

A

saturated and unsaturated

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33
Q

saturated fats prop. and example

A

generally come from animals, solid at room temp. and when ingested in large quantities are linked to heart disease, ex: butter

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34
Q

bonds in sat. fats

A

single bond

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35
Q

unsaturated fats prop. and example

A

extracted from plants, liquid at room temp, healthy dietary fats

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36
Q

bonds in unsaturated fats

A

atleast one double bond formed by removal of H atoms, usually have fewer H atoms than sat fats

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37
Q

exception to unsat. fats having less H atoms than sat fats

A

coconut and palm oil that are saturated

38
Q

steroids

A

don’t have same general structure as other lipids, instead have 4 fused rings

39
Q

steroid examples

A

testosterone and estradiol

40
Q

functions of lipids

A

energy storage, structural, endocrine

41
Q

energy storage

A

1 gram of lipid –> 9 calories, 2x as much as proteins or carbs

42
Q

structural

A

phospholipids (where phosphate group replaces one fatty acid) are major component of cell membrane, cholesterol is an important component of plasma membrane of animal cells

43
Q

endocrine

A

some steroids are hormones

44
Q

phospholipids

A

only 2 fatty acids attached to glycerol backbone, forming two hydrophobic tails

45
Q

phospholipid head

A

has the phosphate and glycerol, phosphate is charged, therefore hydrophilic, when arranged into membrane, stays on the outside

46
Q

proteins

A

complex unbranched molecules, polymers or polypeptides consisted of units called amino acids, which are joined by peptide bonds

47
Q

protein functions

A

growth and repair, signaling form one cell to another, regulation: hormones such as insulin lower blood sugar, enzymatic activity: catalyzing chemical reactions, movement: actin and myosin are protein fibers responsible for muscle contractions

48
Q

dietary sources of protein

A

fish, poultry, meat, plants like beans and peanuts

49
Q

1 gram of pro. ==

A

4 cal

50
Q

elements of proteins

A

CHNOPS

51
Q

amino acids consist of

A

carboxyl group amine group and R variable attached to a central asymmetric carbon atom

52
Q

r group

A

differs with each amino acid, interactions among r groups ultimately determine structure and function of protein

53
Q

fun fact: with only 20 amino acids

A

cells can build thousands of proteins

54
Q

two amino acids with dehydration synthesis

A

form dipeptide, or molecule with two amino acids with one peptide bond

55
Q

conformation

A

shape that determines job performed

56
Q

four levels of protein structure that are responsible for protein’s conformation

A

primary, secondary, tertiary, and quaternary

57
Q

primary structure of a protein

A

refers to the unique linear sequence of amino acids, a slight change in the amino acid sequence can have major consequences

58
Q

Q: sickle cell anemia is caused by the switcharoo of what

A

substitutes valine(GTG) for glutamic(GAG) acid in a molecule of hemoglobin

59
Q

Q: During the 1940s and 50s who was the first man to sequence a protein

A

Fred Sanger

60
Q

What protein did Sanger first sequence and what reward did he receive

A

He sequenced insulin, and received the nobel prize

61
Q

secondary structure

A

results from hydrogen bonding within the polypeptide molecule, refers to how the polypeptide coils or folds

62
Q

two distinct secondary structures

A

alpha helix and beta pleated sheet

63
Q

fibrous proteins

A

proteins that exhibit either alpha helix or beta-pleated sheets or both

64
Q

ex. of fibrous proteins

A

wool, claws, beaks, reptile scales, collagen and ligaments

65
Q

Q: keratin (human hair) is made up of mostly this protein type

A

alpha helizs

66
Q

Q: Silk and spider webs consist of this protein type

A

beta-pleated sheets

67
Q

tertiary structure

A

intricate 3d shape or conformation of a protein that is superimposed on its secondary structure

68
Q

tert. struc. determines

A

protein’s specificity

69
Q

factors that contribute to tert. struct.

A

H bonding btw R groups of amino acids, ionic bonding btw r groups, hydrophobic interactions, Van der Waals interactions, disulfide bonds btw cysteine amino acids

70
Q

quaternary structure

A

proteins that consist of more than one polypeptide chan

71
Q

hemoglobin fact about quat. struct

A

exhibits quat struct. bc it consists of 4 polypeptide chains each forming a heme group

72
Q

specificity def.

A

Chemical specificity is the ability of a protein’s binding site to bind specific ligands. The fewer ligands a protein can bind, the greater its specificity. Specificity describes the strength of binding between a given protein and ligand.

73
Q

factors affecting protein shape, folding

A

pH, salt concentration, temp

74
Q

denaturation

A

these external factors can affect the weak intramolecular forces causes the protein to lose its shape and thus function this is called denaturation

75
Q

basic concept of modern bio

A

protein conformation affects function

76
Q

chaperone proteins or chaperonins

A

assist in folding other proteins

77
Q

prions

A

accumulations of misfolded proteins in brain cells

78
Q

diseases caused by prions

A

Alzheimer’s, Parkinson’s, and mad cow disease

79
Q

3 complementary techniques used to reveal the 3d shape of proteins

A

X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and bioinformatics

80
Q

bioinformatics

A

uses comps and math modeling to integrate the huge volume of data to predict the 3d model of the structure

81
Q

2 nucleic acids

A

RNA and DNA

82
Q

nucleic acid fuction

A

encode all hereditary information

83
Q

Q: info encoded in the sequence of nucleotides in DNA specifies

A

the amino acid sequences of all proteins

84
Q

nucleotide consists of

A

phosphate, 5C sugar (deoxyribose or ribose), and a nitrogen base, (Adenine, Thymine, Cytosine, Guanine, or Uracil)

85
Q

components of org. mol. that are most involved in chemical reactions

A

functional groups

86
Q

how funct. groups are attached

A

to the C skeleton, replacing one or more H atoms

87
Q

Amino group

A

compound name: amino, H-N-H

88
Q

Carboxyl group

A

compound name: carboxyl, O–C-OH

89
Q

Hydroxyl group

A

compound name: alcohol, OH

90
Q

Phosphate group

A

compound name: phosphate, O–P-O-O-O

AP Biology Barron (5 decks)

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