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XIO > Chem ch 18 > Flashcards

Chem ch 18 Flashcards

1
Q

nylon 6.6 (nylon for diane)

A

hexanedioc acid. Nylon 6.6 is a polyamide

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2
Q

CH2 also known as…

A

methylene

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3
Q

polyester is made of what? (polyester must DI from acid and alcohol)

A

diacid and dialcohol

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4
Q

nylon 6.6 has…(carbons)

A

6 carbons in the acid and 6 carbons in the amine

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5
Q

because nylon 6.6 has 2 functional groups…

A

it can go on and on on each end

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6
Q

polyamide is made of

A

diacid and diamine

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7
Q

1,4 benzene carboxylic acid is also called…(benz is treppin)

A

terephthalic acid

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8
Q

terephthalic acid can do____formation with…

A

ester formation with ethylene glycol

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9
Q

terephthalic and ester polymer is called…(pet trep and ester)

A

polyethyleneterephthalate or PET or Dacron

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10
Q

how many naturally occurring amino acids?

A

20

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11
Q

proteins are made up of…

A

amino acids

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12
Q

class of protein based on their job in our body (protein’s job is PC Sshet)

A

1) structural proteins
2) contractile proteins
3) transport protein
4) storage proteins
5) hormone proteins
6) enzymes
7) protection proteins

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13
Q

structural protein ex

A

provides structural compounds, mechanical shape, support ex. collagen (tendons and cartilage) and keratin (skin and hair)

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14
Q

contractile proteins

A

make muscles moves, do mechanical work, ex - myosin and actin

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15
Q

transport protein

A

transports, carries essential substances throughout body ex. hemoglobin

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16
Q

types of transport proteins (2 of them)

A

hemoglobin - globular, transports oxygen

lipoprotein - transports lipids, ex. serum albumin (transports fatty acids)

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17
Q

lipoproteins

A
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18
Q

storage proteins

A

store nutrients and make them available when needed ex. casein - in milk, ferritin - stores iron, myoglobin - stores oxygen and releases when we need it

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19
Q

hormone proteins

A

regulates body metabolism ex. - insulin, growth hormone

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20
Q

enzymes

A

catalyze biochemical reaction in the cell

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21
Q

naming enzymes

A

most end with “ase” ie - sucrase: catalyzes hydrolysis of sucrose. Not all have this naming - trypsin - catalyzes the hydrolysis of protein. ie - amylase - begins catalyzing digestion of carbohydrates

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22
Q

protection proteins

A

recognize and destroy foreign substances, ie - immunoglobulins - stimulates immune response

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23
Q

amino acids

A

have amino and acid group - all have this basic structure
H
|
H2N _ C _ COOH
|
R (this is the side chain, 20 of them)

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24
Q

how many side chains?

A

20 different, give unique identity to amino acids

it determines it’s function

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25
Q

amino acids have…

A

name, 3 letter code, one letter code and number

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26
Q

has an acid and a base in the same molecule

A

amino acid

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27
Q

zwitter ion

A

has equal positive and negative charges. depends on the ph of the solution

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28
Q

only zwitter ions are found…

A

in our body. the full amino acid formula is not in our body, it changes to zwitter

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29
Q

you can tell if it’s a zwitter ion if..

A

there is a + and - charge on the compound

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30
Q

if you have a zwitter ion in acidic solution (H+)

A

the H+ will turn the COO- to positive, making it COOH.

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31
Q

amino acids in acidic solutions are positive or negative?

A

positively charged

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32
Q

amino acid in basic solution (you don’t want to be basic)

A

H2N - C - COO-. The OH- will take a hydrogen from the N3H, making it N2H. it is negatively charged.

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33
Q

at any pH, the amino acid is in it’s…

A

zwitter form. This Ph is called PI = isoelectric point

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34
Q

in isoelectric form (PI), the net charge is…

A

zero.

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35
Q

the PI point for amino acids depends on the…

A

nature of R group

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36
Q

9 amino acids that are…

A

nonpolar - neutral

ie H, CH3, CH(CH3)2, benzene, gylcine, alanine, valine, phenylalanine

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37
Q

valine (val has a friend named iso)

A 
neutral and nonpolar 
          H
            |
H2N - C - COO-
            |
           C
        /        \
    CH3      CH3
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38
Q

classes of amino acids

A

1) neutral and nonpolar
2) neutral and polar
3) acidic amino acids
4) basic amino acids

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39
Q

polar and neutral amino acids (OH c=osh Oh, coosh ball is neutral at the north pole)

A

it will either have an OH or SH group, OR an C=O attached to NH2 group. The NH2 in the neutral amino will be attached to a C=O-O group to balance it out.

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40
Q

how many amino acids are polar?

A

6 amino acids

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41
Q

how many acidic amino acids?

A

2 - they have an additional COO- group in the R group - Look at the side chain to identify

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42
Q

acidic amino acids are positively or negatively charged? (opposite acid)

A

negatively, bc they have 2 COO-

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43
Q

how many basic amino acids?

A

only 3, they have additional NH3+ group in the R group (look at the side chain to identify)

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44
Q

are basic amino acids positively or negatively charged? (basically positive)

A

positively

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45
Q

R group can be…

A

hydrophobic or hydrophilic

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46
Q

MEMORIZE

A

glycine structure

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47
Q

the number after the amino acid…

A

tells the pH in which the acid is in zwitter ion form

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48
Q

MEMORIZE

A

structure of cysteine

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49
Q

acid makes you feel…

A

low

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50
Q

how many amino acids have a chiral center?

A

19 - all except gylcine. The 19 are also D or L

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51
Q

D (Elle likes amino acids)

A

only L-amino acids are selected to make proteins by nature

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52
Q

D and L is only based on the…

A

amino group, H3N+. If the amino group is on the left, it’s L-amino acid, right it’s D-amino acid

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53
Q

D an L isomers are called…ex. L-Alanine and D-alanine

A

two enantiomers

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54
Q

intermolecular forces (the intermolecular force SHILD)

A 
non-covalent forces - 
1) H-bonding 
2) vander waals forces or london dispersion 
3) ionic bonding - ions in R chain 
4) disulfide bond - S-S
Polar
5) dipole dipole
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55
Q

additional COO or H3N makes a..(add some salt)

A

salt bridge

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56
Q

all amino acids have…(their make up)

A

a carboxylic group, an amine group, an R side chain, and an H all attached to central carbon

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57
Q

The principal classes of biomolecules are (PLNC)

A

proteins, carbohydrates, lipids, and nucleic acids

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58
Q

proteins do what for living things?

A 
They provide structure (keratin) and support (actin filaments) to tissues and organs throughout our bodies.
As hormones (oxytocin) and enzymes (catalase), they control aspects of metabolism
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59
Q

In body fluids, water-soluble proteins pick up other…

A

molecules for storage (casein) or transport (transferrin, Fe3+).

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60
Q

Proteins of the immune system provide

A

protection (Immunoglobulin G) against invaders, such as bacteria and viruses

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61
Q

proteins are polymers of what?

A

amino acids

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62
Q

Amino acids in proteins are located where?

A

alpha-amino (α-amino) acids because the amine group in each is connected to the alpha carbon

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63
Q

For 19 of these amino acids…

A

only the identity of the side chain attached to the carbon differs

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64
Q

The remaining amino acid not like the others..

A

proline, is a secondary amine whose nitrogen and carbon atoms are joined in a five-membered ring

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65
Q

The 20 α-amino acids that make up proteins are classified as…

A

neutral, acidic, or basic, depending on the nature of their side chains

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66
Q

The 15 neutral amino acids are further divided into…

A

those with nonpolar side chains and those with polar functional groups, such as amide or hydroxyl groups in their side chains

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67
Q

what enables proteins to perform their functions?

A

The sequence of amino acids in a protein and the chemical nature of their side chains

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68
Q

The intermolecular forces present between amino acids or between protein chains are (hivd)

A

hydrogen bonding, Van der Waals forces, ionic bonding, and disulfide bonds

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69
Q

The nonpolar side chains are described as hydrophobic or hydrophilic?

A

hydrophobic (water-fearing). To avoid aqueous fluids, nonpolar side chains gather into clusters to create a water-free environment.

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70
Q

The polar, acidic, and basic side chains are hydrophobic or hydrophilic?

A

The polar, acidic, and basic side chains are hydrophilic (water-loving). Attractions between water molecules and hydrophilic groups on the surface of folded proteins impart water solubility to the proteins

71
Q

how many amino acids are chiral?

A

19, only gylcine is achiral

72
Q

α-amino acids can exist as…(Lane likes the natural look)

A

D- or 
L-enantiomers.

Nature selectively uses only L-amino acids for making proteins

73
Q

zwitter ion

A

A neutral dipolar ion that has one positive charge and one negative charge

74
Q

because amino acids contain an acid and basic part, they can..

A

undergo an intramolecular acid-base reaction to form a zwitterion

75
Q

intermolecular acid-base reaction gives amino acids many of the physical properties of…

A

salts: crystals, high melting points, and water solubility.

76
Q

In acidic solution, amino acid zwitterions…

A

accept protons on their basic –COO– groups to leave only the positively charged –NH3+ groups

77
Q

In basic solution, amino acid zwitterions…

A

lose protons from their acidic –NH3+ groups to leave only the negatively charged –COO– groups.

78
Q

The isoelectric point (pI)describes…

A

the pH at which a sample of an amino acid has equal numbers of + and – charges

79
Q

at the pI point…

A

the net charge of all the molecules of that amino acid in a pure sample is zero

80
Q

Isoelectric points influence…

A

protein solubility and determine which amino acids in an enzyme participate directly in enzymatic reactions.

81
Q

A dipeptide results from the formation of…(peppy opposites)

A

a peptide bond between the –NH2 group of one amino acid and the 
–COOH group of a second amino acid.

82
Q

Three amino acids linked by peptide bonds will form..

A

a tripeptide

83
Q

Any number of amino acids can link together to form a…

A

linear, chainlike polymer—a polypeptide.

84
Q

Very large peptides (oligopeptides) contain..

A

hundreds of amino acids and are referred to as proteins.

85
Q

A pair of amino acids can be combined to form…

A

two different dipeptides

86
Q

Peptides and proteins are always written with the…

A

amino­-terminal amino acid (N-terminal, the one with the free –NH3+) on the left and carboxyl-terminal amino acid (C-terminal, the one with the free –COO–) on the right.

87
Q

The individual amino acids joined in the chain are referred to as..

A

residues

88
Q

peptide naming

A

name the amino acid residues in order, starting at the N-terminus and ending with the C-terminus.

89
Q

Primary structure (primary is most important)

A

Primary structure

is the sequence of amino acids in a protein chain.

90
Q

Along the backbone of a protein is a…

A

chain of alternating peptide bonds and α-carbon atoms.

91
Q

The amino acid side chains are located where?

A

substituents along the backbone, where they are bonded to the α−carbon atoms

92
Q

The spatial arrangement of the polypeptide backbones of proteins determines…

A

secondary protein structure (2°)

93
Q

The secondary structure includes…(2nd set of sheets)

A

wo kinds of repeating patterns known as the alpha-helix (α-helix) and the beta-sheet (β-sheet)

94
Q

what holds the polypeptide chain in place? (What holds everything in place)

A

Hydrogen bonding between backbone atoms holds the polypeptide chain in place

95
Q

Alpha-helix (α-helix)

A

A secondary protein structure in which a protein chain forms a right-handed coil stabilized by hydrogen bonds between peptide groups along its backbone

96
Q

Beta-sheet (β-sheet)

A

A secondary protein structure in which adjacent protein chains either in the same molecule or in different molecules are held together by hydrogen bonds along the backbones, forming a flat sheetlike structure

97
Q

Proteins are classified in several ways..(fg proteins)

A

one of which is to identify them as either fibrous proteins or globular proteins

98
Q

Fibrous protein

A

A tough, insoluble protein whose protein chains form fibers or sheets

99
Q

Globular protein (glob likes water)

A

A water-soluble protein whose chain is folded in a compact shape with hydrophilic groups on the outside

100
Q

Tertiary protein structure (3°)

A

The way in which an entire protein chain is coiled and folded into its specific three-dimensional shape

101
Q

native protein

A

A protein with the shape in which it functions in living systems

102
Q

simple protein (simple residue)

A

A protein composed only of amino acids ex. ribonuclease

103
Q

salt bridge

A

Where there are ionized acidic and basic side chains, the attraction between their positive and negative charges creates salt bridges

104
Q

Amino acids with charged R groups will interact with…

A

water through hydrogen bonding

105
Q

Hydrocarbon side chains are attracted to each other by which forces?

A

dispersion forces (primarily london dispersion), which can create a water-free pocket in the protein chain

106
Q

Cysteine amino acid residues have side chains containing…

A

Cysteine amino acid residues have side chains containing thiol functional groups (–SH) that can react to form sulfur-sulfur bonds (–S–S–)

107
Q

Disulfide bond

A

An S–S bond formed between two cysteine side chains that can join two separate peptide chains, or cause a loop in a single peptide chain

108
Q

Ribonuclease is classified as a…

A

simple protein because it is composed only of amino acid residues

109
Q

Conjugated amino acid has…(like a conjugated verb)

A

non-amino acid group in it, like hemoglobin or myoglobin - the heme group is the non-amino group.
casein - milk protein, has phosphate so it’s conjugated also.
lipoprotein - has lipids added
glycoproteins - have carbohydrate group in it

110
Q

Quaternary protein structure (the final quarter)

A

Quaternary protein structure is the way in which two or more protein chains aggregate to form large, ordered structures

111
Q

Polypeptides are primarily held together by ___forces

A

noncovalent forces, but covalent bonds and 
non–amino acid portions may also be incorporated

112
Q

hemoglobin - hydrophilic or phobic?

A

The arms are hydrophilic, inside is hydrophobic.

a conjugated quaternary protein composed of four polypeptide chains (two each of two polypeptides called α-chain and β-chain) held together by hydrophobic interactions and four heme groups

113
Q

hemoglobin in the lungs (and can carry how many molecules?)

A

O2 binds to Fe2+ so that each hemoglobin can carry a maximum of four O2 molecules

114
Q

hemoglobin in tissue

A

In tissues in need of oxygen, O2 is released, and CO2 is picked up and carried back to the lungs

115
Q

Hemoglobin is what type of protein? (not globular)

A

a cellular protein, normally found only inside cells and carried throughout the body inside red blood cells

116
Q

Serum albumin is what type of protein?

A

it is referred to as a mobile protein because it is dissolved in an extracellular (outside the cell) fluid. It carries CO2 to the lungs for disposal

117
Q

Collagen is the major part of what tissues?

A

connective tissues

118
Q

The basic structural unit of collagen (tropocollagen) is…

A

three intertwined chains of about 1000 amino acids each. Each chain is loosely coiled in a left-handed (counterclockwise) direction

119
Q

Primary structure is the…

A

sequence of amino acids connected by peptide bonds in the polypeptide chain, for example, Asp-Arg-Val-Tyr

120
Q

Secondary structure is the

A

arrangement in space of the polypeptide chain, which includes the regular patterns of the α-helices and the β-sheet motifs (held together by hydrogen bonds between backbone carbonyl and amino groups in amino acid residues) plus the loops and coils that connect these segments

121
Q

Tertiary structure is the

A

folding of a protein molecule into a specific three-dimensional shape held together by noncovalent interactions primarily between amino acid side chains that can be quite far apart along the backbone and, in some cases, by disulfide bonds between side-chain thiol groups

122
Q

Quaternary structure is…

A

two or more protein chains assembled in a larger three-dimensional structure held together by noncovalent interactions

123
Q

Digestion of proteins in the diet involves…(Need water to digest)

A

hydrolyzing peptide bonds in the stomach and small intestine, where the process is catalyzed by enzymes. Amino acids are absorbed through the wall of the intestine

124
Q

Denaturationis the loss of…(you can’t denature the first evil)

A

secondary, tertiary, and quaternary protein structure that leaves primary structure intact because the peptide bond isn’t broken.

125
Q

Solubility is often decreased by…

A

denaturation. Enzymes lose their catalytic activity and other proteins are not able to carry out biological functions when denatured

126
Q

Most denaturation is irreversible or reveresable?

A

Most denaturation is irreversible, but renaturation is accompanied by recovery of biological activity

127
Q

agents that cause denaturation (heat the mechanic)

A

Heat—The weak side-chain attractions in globular proteins are easily disrupted by heating.
Mechanical agitation—The most familiar example of denaturation by agitation is the foam produced by beating egg whites. Denaturation of proteins at the surface of the air bubbles stiffens the protein and causes the bubbles to be held in place

128
Q

agents that cause denaturation 2 (even clean organic fruit)

A

Detergents—Even very low concentrations of detergents can disrupt the association of hydrophobic side chains.
Organic compounds—Polar solvents interfere with hydrogen bonding by competing for bonding sites.

129
Q

agents that cause denaturation 3 (sweat salt)

A

pH change—Excess H+ or OH– ions react with basic or acidic side chains in amino acid residues and disrupt salt bridges.
Inorganic salts—High concentrations of ions can disturb salt bridges

130
Q

the only acidic amino acids are…(ooh acid)

A

asperatic and glutamic - don’t need to remember, BUT the both have O= and OH as part of the side chain, which makes them acidic

131
Q

the basic amino acids will always have…

A

a N in the side chain

132
Q

alkyl side chain has…

A

ONLY C and Hs in it

133
Q

at a low pH (acidic) basic groups would gain or lose an H+?

A

gain an H+

134
Q

at a high pH, acids may gain or lose an H+? (high is the opposite on acid)

A

lose an H+, so HN3 becomes HN2

135
Q

naming peptides

A

change last part to yl for all except the one at terminal C - keep that the full name. ex - alanine gylcine would be alanyl-glycine

136
Q

each amino acid is a residue, so in tripeptide we have how many residues?

A

3

137
Q

2-20 amino acids are called…(2 olga!)

A

oligopeptides

138
Q

more than 20 amino acids are called…

A

proteins or polypeptides

139
Q

quatranary structure can have how many chains of amino acids?

A

2, 3, or 4

140
Q

both alpha and beta sheet are stabilized by what?

A

H bonding

141
Q

the arrangement in beta sheets is which direction?

A

anti-parallel - this just means that the shape rotates C and N terminals at the curve. The C and Ns are facing each other.

142
Q

keratins have mostly what structure? (KERATIN think opposite)

A

alpha helix - so they have a secondary structure

143
Q

fibroin

A

silk, spider webs. has beta sheet structure

144
Q

globular proteins are in what shapes?

A

globe-like 3-dimensional, some are alpha helix and/or beta sheet that is folded.

145
Q

most enzymes are what proteins?

A

globular

146
Q

forces in tertiary and quatranary structures only (tert and quat take LSD H)

A

Non-covalent forces***london forces, ionic forces - or salt bridge, and H-bonding, and disulfide (only with cysteine)

147
Q

2 classifications based on location - on the move or staying put?

A

1) cellular and 2) mobile

148
Q

mobile proteins

A

soluble and therefore globular. they are located on extra-cellular, which just means outside the cell. mostly carry CO2 from tissue to lungs

149
Q

cellular protein

A

formed in cell

150
Q

most abundant protein in mammals is…

A

collagen (30% of total protein)

151
Q

collagen is globular or fibrous?

A

it is fibrous, made of 3 chains

152
Q

where is collagen found in the body? (collagen cast baby CST BB)

A

skin, tendons, bones, blood vessels and connective tissue

153
Q

what structure is collagen? (collagen is complex)

A

quatrenary

154
Q

what structure is insulin?

A

quatrenary

155
Q

what causes denaturation? (denature the MD at IHOP)

A

heat, mechanical (whisk), organic compound (adding vinegar to milk), inorganic salt, pH change, detergent.

156
Q

the amino acid sequence naming is…

A

just the 3 letter abbreviation

157
Q

how to tell if an amino acid side chain is non polar

A

the side chain will be MOSTLY C and H groups - 2 have Ns in the ring, but the majority of the side chain will be C and H

158
Q

how to tell if a polar amino acid side chain is acidic

A

There are only 2 - it will have a C=O O group in the side chain, and the ending of the name will be acid

159
Q

how to tell if a polar amino acid side chain is basic

A

it will have an NH2, NH3 or an N NOT attached to C=O or inside a cyclic. Inside a cyclic is not basic.

160
Q

how to tell if an amino acid side chain is polar and neutral

A

it will either have an OH or SH group, OR an C=O attached to NH2 group

161
Q

to figure out what type of bond will form, look at the…

A

side chains. 2 non-polar will form hydrophobic, acidic or basic and a neutral will form a salt bridge, and

162
Q

if a C has a CH2, it cannot be…

A

chiral

163
Q

the backbone of alpha helix and beta sheet is held together by what bonds?

A

hydrogen bonds

164
Q

alpha helix is globular or fibrous?

A

both

165
Q

beta sheets are globular or fibrous?

A

fibrous

166
Q

tertiery structure is connected by what?

A

side chains. Alpha and beta are connected by amide and C=O bonds.

167
Q

asparagine one letter code (No asperagus)

A

N

168
Q

glutamine one letter code (Qnon glut)

A

Q

169
Q

tyrosine one letter code (why tyro?)

A

Y

170
Q

aspartic acid one letter code (Don’t be asperatic spaz)

A

D

171
Q

glutamic acid one letter code (Exclude gluten, mic)

A

E

172
Q

arginine one letter code (aRRR pirate)

A

R

173
Q

lysine one letter code (Kut lyse)

A

K

174
Q

examples of quaternary structures

A

hemoglobin and collagen

XIO (372 decks)

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