Topic 3 Flashcards

(92 cards)

1
Q

what are all composed of carbon compounds

A

proteins, DNA, carbohydrates

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2
Q

organic chem

A

study of compounds that contain carbon, regardless of orgin
- usually contains H as well

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3
Q

what are the major elements of life

A

c, h, n, s, p
- reflects the common evolutionary orgin of all life

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4
Q

how many bonds can carbon form

A

4
creates a versatility
- infinite number of combinations of molecules

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5
Q

what are the most common carbon atoms bond to

A

H O N

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6
Q

carbon chains form

A

skeletons or organi molecules
- vary in length and shape
- making large complex molecules possible

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7
Q

diversity in carbon skeletons

A

length
branch location
double bond location
presence of rings

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8
Q

isomers

A

same molecular formula but different structures and properties

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9
Q

structural isomers

A

different covalent arrangments of atoms

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10
Q

cis-trans isomers

A

same covalent bond but differ in their spatial arrangments

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11
Q

enaantiomers

A

isomers that are mirror images of each other
- can have different levels of bioloical acitivity

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12
Q

functional groups

A
  • chemical groups involved directly in chem reactions
  • based off number, shape, arrangement, charge
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13
Q

estradiol and testosterone example

A
  • sex hormones, drastically different bioloical outcomes but differ only by two functional groups
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14
Q

seven important functional groups in the chem of life

A

1 hydroxyl group
2 carbonyl group
3 carboxyl group
4 amino group
5 sulfhydryl group
6 phosphate group
7 methyl group

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15
Q

hydroxyl group

A
  • polar due to electronegative O
  • forms bonds with water
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16
Q

carbonyl group

A

c double bonded to O

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17
Q

carboxyl group

A

c double bonded to O
c bonded to OH

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18
Q

amino group

A

NH2

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19
Q

sulhydryl group

A

two SH groups can react forming a cross link that helps to stabalize protein structure

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20
Q

phosphate group

A
  • contributes negative charge
  • when attached, confers ability to react with water, releasing energy
    ex ATP
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21
Q

methyl group

A
  • affects gene expression
  • affects shape and function of sex hormones
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22
Q

atp

A

adenosine triphosphate
- adenosine attached to a string of phosphate groups
- ato stores potential to react with water
- this energy is used by the cell

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23
Q

all living organisms are made up of

A
  • carbohydrates
  • lipids
  • proteins
  • nucleic acids
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24
Q
  • carbohydrates
  • proteins
  • nucleic acids
    are considered what
A

macromolecules. not lipids

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25
monomer
repeating units that serve as builiding blocks - nucleotides, amino acids, monosaccarides
26
polymer
long molecule consisting of many monomers - carbohyrates, proteins, nucleic acids - provides large variety from small set of monomers
27
dehydration synthesis reaction
creates a polymer from monomer subunits. - removes the water from monomers (the ending H + OH) - the monomers are joined where H and OH were removed
28
hydrolisis reaction
- splits water into H and OH - H added to one monomer, OH to the other - monomers are released by the addition of the water molecule - degrades polymer into monomers
29
carbohydrates
sugars and polymers of sugars
30
monosaccarides
simple carbohydrates
31
polysaccarides
complex carbohydrates, polymers
32
gluclose
most common monosaccaride - fructose, galactose are isomers (same formula, diff structure) - fuel - classified by number of carbons
33
disaccharide
two monosaccarides come together through dehydration synthsis
34
glycosidic linkage
covalent bond between two monomers - can build a variety of dissachharides and polysacchaides
35
starch
- storage of polysaccharides of plants - glucose monomers in a helical structure - simpliest form of starch is amylose
36
what is energy stored as plant
starch
37
whenn sugar is needed for cells what happens
polysaccharides are hydrolyzed to release gluclose monomers - animals have enzymes that can hydroloze plant starch
38
glucose polymers in animals stored as
glycogen - stored in muscle and liver cells as short term energy reserve - multiple branching points for easy use
39
cellulose
major component of the tough wall of plant cells - glucose monomers in a straight and unbranched structure - insoluble fiber
40
lipids
- not a macromolecule, not a plymer - hydrophobic due to hydrocarbon regions (non polar) - fats, phospholipids, steroids
41
hydrocarbons
organic molecule consisting of only C and H ex CH4 - fats have hydrocarbon components, so does petroleum - can undergo reactions that release a large amount of energy
42
fats are composed of
glycerol: 3 carbon alcohol with three hydroxyl groups - fatty acid: carboxyl group attached to a long carbon skeleton
43
fats are hydro...
phobic. they separate from water. water molecules hydrogen bond to each-other and exclude the fats
44
triacylglycerol or triglyceride
three fatty acids joined by glycerol by an ester linkage
45
fatty acids within a fat
be all the same or all different vary in length vary in number and location of double bonds
46
saturated fatty acids
maximum number of hydrogen atoms possible - Solid at room temp - no double bonds - FA tails are straight, more dense therefore, dense - most animal fats are saturateed
47
unsaturated fatty acidsONE OR MORE DOUBLE BONDS
- liquid at room temp - at least one double bond - fewer hydrogen present - the tails are less tight, less dense - plant and fish fats are usually unsaturated
48
trans fats
made by hydrogenating veg oils - straight, pack tighter, solid
49
fats
major function is stored energy - animals store fat in adipose cells (cushion vital organs insulate body)
50
phospholipid
- two fatty acids and a phosphate group are attached to glycerol - form cell/plasma membrane
51
amphipathic
- FA tails are hydrophobic - phosphate group forms hydrophilic head
52
steroids
lipids characterized by carbon skeleton consisting of four fused rings
53
cholesterol
- component in animal cell membranes - a percursor from which steroids are synthesized
54
proteins
macromolecule - polymer made of monomers know an amino acids - 50% of dry madd in cells - made of 20 amino acids - consists of one or more polypeptides
55
amino acid
organic molecules with amino and carboxyl group - differ in their properties die to R group
56
polypeptides
unbranched polymers built from these amino acids
57
non polar side chains (amino acid group)
hydrophobic 9 of them
58
polar side chains (amino acid groups)
hydrophilic 6 of them
59
charged side chains (amino acid groups)
- acidic (neg charge) - basic (pos charge)
60
how are amino acids linked
peptide bonds
61
what is a polypeptide
polymer of amino acids - each polypeptide has a unique linear sequence
62
what do peptide bonds create
polymers with carboxly end (c terminus) and an amino acid end (N terminus)
63
enzymes
proteins tha tspeed up chem reactions often end in ase
64
defensive proteins
protection against disease - antibodies to destory viruses
65
storage proteins
storage of amino acids - protein of milk major source of amino acids for baby animals
66
transport proteins
transport hemoglobin transport iron
67
hormonal proteins
coordination of an organisms activities insulin, take up gluclose regulating blood sugar
68
receptor proteins
response of a cell to chemical stimuu - recpeots bullt into membrane that pick up neurotransmitters
69
structural proteins
support keratin protein of hair
70
contractile and motor proteins
movement responsible fo cilia and flagella movement
71
primary structure
one of four levels of structure - unique sequence of amino acids - determined by inherited genetic info - n and c terminals - can be written in 3 letter codes
72
secondary structure
2/4 of the levels of structure of proetins - constists of coils and folds in the polypeptide chain - alfa helix (coil, held together through hydrogen bonding) - beta sheets (hydrogen bonding occurs between pleated sheets
73
tertiary structure
3/4 levels of structure of proteins - overall 3d shape of a polypeptide -stabalized by interactions between various side chains (r groups) - groups of hydrophilic residues - gorups of polar charged residues - disulfide bridges (cysteine)
74
quaternary structure
4/4 of the levels of structure of a protein - results when a protein consists of multple polypeptide chains - collagen - hemoglobin
75
sickle cell anemia
- tiny chnages in primary structure sequence can affect protein structure and function - hemoglobin- oxygen transporter in out blood - sickle cell anemia- inherited blood disorder due to sing aa substitution
76
sickle cell anemia fact
allows for malaria resistance when heterozygous
77
determinants of protein structure
- proteins often have several structure before final product - physical and chem conditions (pH, salininty, temp)
78
denaturation
loss of protein structure, becomes biologically inactive
79
nucleic acids
store, transmit, express hereditary info
80
dna
deoxyrionucleic acid - sugar is deoxyribose
81
rna
sugar is ribose
82
genes
consists of dna - polymer made from monomers (nucleotides) - provides direction for its own replication - directs synthesis of messanger rna - using mrna, controls protein sythesis>gene expression
83
nucleic acid are polymers, made from monomers called
nucleotides
84
each nucleotide contains
- nitrogen base, pentose sugar, phosphate group - nitrogenous base -> nucleoside -> nucleotide
85
two families of nitrogenous bases
pyrimidines purines
86
pyrimidines
cytosine, thymine, uracil - single sic membered ring
87
purines
adenine and guanine - six membered ring fused to five-membered ring
88
creating nucleotide polymers
- sugar phosphate backbone with nitrogen base - nucleotides are linked together by phosphodiester linkage - each backbone has 5' and 3' end
89
dna structure
- two antiparallel (run in opposite direction) backbones, double helix
90
base pairing dna
A + T C + G - complementary base pairing
91
base pairing rna
A + U C + G
92
in rna complemntary base pairing can occur
- between two rna molecules - between parts of the same molecule - 3d structure of rna is more variable