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UT BCH 369 > Final Exam > Flashcards

Final Exam Flashcards

1
Q

citric acid cycle products

A

3 NADH, 1 FADH2, 1 GTP/ATP, 2 CO2

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2
Q

regulatory enzymes in citric acid cycle

A

isocitrate dehydrogenase (+ for ADP, - for NADH and ATP)

alpha-ketoglutarate dehydrogenase (- for NADH, ATP, succinyl CoA)

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3
Q

high succinyl coA will slow down…

A

ETC

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4
Q

dehydrogenase catalyzes…

A

an oxidation step

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5
Q

oxidation steps in citric acid cycle

A

4; 1 produces FADH2, 3 produce NADH

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6
Q

high ADP means energy is…

A

low

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7
Q

can i keep selling seashells for money officer?

A

pneumonic for citric acid cycle

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8
Q

acetyl-CoA starts the…

A

citric acid cycle

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9
Q

dehydrogenases in citric acid cycle

A

I AcKnowledge, SUCky Men

Isocitrate
Alpha-Keto
SUCcinate
Malate

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10
Q

ETC: 1 NADH creates…

A

2.5 ATP

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11
Q

ETC: 1 FADH2 creates…

A

1.5 ATP

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12
Q

proton gradient from ETC is in…

A

intermembrane space

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13
Q

NADH and FADH2 comes from…

A

mitochondrial matrix

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14
Q

complex I

A

NADH

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15
Q

complex II

A

FADH2

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16
Q

what happens to electrons as they pass through ETC?

A

they become lower and lower in free energy hence why they are passed on

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17
Q

final electron acceptor

A

removes low energy electron and binds them to free H+ to form water

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18
Q

synthesis of ATP in mitochondria is driven by…

A

a protein gradient

reoxidation of NADH and FADH2 indirectly creates a protein gradient

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19
Q

ATP synthase

A

“complex V”

carnival ride (subunit C) - loads H+ and rotates to power the rest

beta subunit - ATP produced

alpha subunit - stabilize the beta subunits

loose: ADP and inorganic phosphate (Pi) are mingling (ADP + Pi)

tight: ADP and Pi bind to produce ATP

open: ATP released

conformations change by rotating of the gamma stalk caused by rotating of C subunit

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20
Q

stator

A

holds ATP synthase in place

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21
Q

E cell

A

E red - (E ox)

PLUG IN AS GIVEN

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22
Q

what is oxidized? what is reduced? spontaneous reaction?

A

OIL RIG - use this to figure out what goes on which side of balanced equation

pick the half reaction with more negative potential (lower E value) will be oxidized

greater E value will be reduced

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23
Q

g deg: phosphorylase action

A

MAIN ENZYME: asdjfa;dkj

cleaves alpha 1,4 linkages and creates glu-1-phosphate

will cleave 7-8 glucose monomers (whatever is 4 monomers away from the branch)

glu-1-phos –> glu-6-phos by phos

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24
Q

phosphoglucomutase

A

g1p –> g6p

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25
Q

branch of glycogen

A

alpha 1,6 linkage

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26
Q

g6p + water

A

glucose + inorganic phosphate

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27
Q

once glycogen cleaved by g1p…

A

4 glucose monomers still attached - NOT wanted!

transferase! takes 3 from the end and puts on end of glycogen chain

alpha 1,6 glucosidase cleaves using water to create FREE GLUCOSE with the one that remained after the transferase passed through

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28
Q

after degradation, phosphorylase…

A

keeps cleaving the glycogen chain until it reaches the core

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29
Q

glycogen synthesis

A

MAIN ENZYME: glycogen synthase

first, need to activate! with UDP glucose (glucose + UTP = UDP)

synthase transfers glucose from UDP glucose onto growing chain

glycogenin is the CORE - autoglycosylation can also transfer glucose (essentially, can participate in chain elongation)

adds 7-8 monomers to core

long chain isn’t convenient!! we must branch

branching enzyme! takes added glucose monomers and creates alpha 1,6 linkage to the 4th carbon from the right end of the core

next branching point much be at least 4 units away from the last branching points

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30
Q

a to b

A

covalent modification (something is getting phosphorylated)

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31
Q

T to R

A

allosteric modification (something about external factors will affect being pushed into these states)

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32
Q

most active

A

phosphorylase a (phosphorylated) in R state

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33
Q

least active

A

phosphorylase b in T state

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34
Q

T state

A

active site is covered

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35
Q

phosphorylase b

A

not phosphorylated

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36
Q

liver is source of…

A

glucose mobilized between meals; liver stores glucose

phosphorylase a is dominant

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37
Q

muscle…

A

energy reserve for muscle control; muscle CANNOT supply glucose because it does not contain glucose-6-phosphatase

phosphorylase b is dominant

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38
Q

high conc of glucose reverts…

A

R to T state since a high conc of glucose means that the liver doesn’t need to call on glycogen stores

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39
Q

high AMP means we need energy

A

R state which pushes forward glycogen degradation

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40
Q

high ATP means…

A

energy is needed

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41
Q

what does protein kinase A do?

A

phosphorylates!!

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42
Q

reciprocal regulation of glu deg and syn

A

protein kinase A and protein phosphatase 1

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43
Q

protein kinase A

A

phosphorylates through turning on kinases

glycogen phosphorylase (b–>a)

glycogen synthase (a–>b)

starts the breakdown of glycogen because we need energy in the form of free glucose

phosphorylase <3 phosphorylation

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44
Q

protein phosphatase 1

A

dephosphorylates!

glycogen phosphorylase (a–>b)
glycogen synthase (b–>a)

starts glycogen synthesis to make glycogen and remove stores of free glucose

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45
Q

hormones

A

act on kinases

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46
Q

insulin

A

means high glucose level

start glucose synthesis

glycogen synthase kinase!! will become inactivated when insulin is high to produce glycogen to keep synthase in the a state

inactivated by covalent modification through phosphorylation

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47
Q

glucagon and epinephrine

A

send out same signal

low glucose level (glucose is gone)

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48
Q

phosphorylatine

A

activates phosphorylase kinase BUT inactivates

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49
Q

glycogenesis enzymes

A

glycogen synthase

branching enzyme

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50
Q

glycogenolysis

A

glycogen phosphorylase

transferase

alpha 1,6 glucosidase

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51
Q

PPP phases/products

A

phase 1: oxidative phase - make NADPH

phase 2: non oxidative phase - makes 5C sugars (ribose-5-phosphate)

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52
Q

mode 1

A

when we need ribose 5 phosphate MORE than NADPH

non-oxidative phase

cell division since r5p is needed MUCH more

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53
Q

mode 2

A

need ribose 5 phosphate and NADPH equally

oxidative phase then an isomerase to transform ribulose to ribose

ex: when cell is rapidly dividing since r5p is needed for nucleotide materials and NADPH for biosynthetic needs - would more need r5p MORE but still “equal” - acceptable answer according to labrake

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54
Q

mode 3

A

need lots of NADPH&raquo_space; r5p

oxidative state - easy

isomerase will create r5p but we do not need it!

end up with glycolysis intermediates that can go into further oxidative steps go into gluconeogenesis (??)

repeat until cell is happy

needed when synthesizing fatty acids

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55
Q

mode 4

A

need NADP and ATP

oxidative state

glycolysis intermediates and go forth with glycolysis

will create pyruvate for citric acid cycle and electron transport chain to make ATP

needed during oxidative stress

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56
Q

NADPH

A

reduces reactive oxidative species

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57
Q

PPP effectors

A

NADP+ (+)

fatty acid acyl CoA (-)

NADPH (-)

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58
Q

first step of PPP

A

dehydration of glucose-6-phosphate

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59
Q

how much more ATP is generated from glucose-6-phosphate, compared to glucose, when it is metabolized by the glycolytic pathway?

A

1

glycolysis: 4 ATP products- 2 ATP react = 2 net ATP

starting at g6p: 4 - 1 = 3

therefore 1 more is generated

why? we skip the first reaction that takes an ATP (????)

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60
Q

glutathione protects against

A

reactive oxidative species

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61
Q

fatty acid synthesis

A
  1. transport from mitochondria: acyl-conitine
  2. activation
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62
Q

acc1 and 2

A

regulated covalently and allosterically

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63
Q

acc1

A

cytosol

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64
Q

acc2

A

mitochondria

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65
Q

inhibition of acc2 will…

A

push forward beta oxidation; therefore, negative effectors of acc2 will push it forward

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66
Q

fatty acid synthesis

A

acetyl coA in mitochondria is converted to citrate and transported to cytoplasm where it is reconverted

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67
Q

insulin dephos….

A

acc1 and acc2 become active

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68
Q

activation of FA

A

acyl-coA synthetase - ATP is required

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69
Q

steps of beta oxidation

A

oxidation

hydration

oxidation

thiolase

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70
Q

products of beta oxidation

A

1 nadh, 1 fadh, 1 acyl coa

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71
Q

example where glucose in the body is low: prolonged starvation

A

ketone bodies can be used as alt source of energy!

especially important for the brain!

keto diet is meant for epilepsy

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72
Q

nutritional ketosis

A

not that bad but can’t last forever because it makes the blood acidic

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73
Q

ketoacidosis

A

dangerous for individuals with type 1 diabetes

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74
Q

which ketone body contributes the most energy

A

3-hydroxybutyrate

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75
Q

complex that does not contribute to proton gradient

A

complex ii

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76
Q

ribosome

A

site of protein synthesis

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77
Q

mitochondria

A

generates energy

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78
Q

cytoplasm

A

solution of water, nutrients, and proteins

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79
Q

nucleus

A

controls and regulates the activity of the cell

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80
Q

types of intermolecular forces present between h and o

A

van der waals forces, dipole-dipole, hydrogen bond

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81
Q

hydrogen bonds

A

special type of dipole-dipole attraction between molecules, NOT a covalent bond to a hydrogen atom

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82
Q

hydrogen bond acceptor

A

atom, ion, or molecule component of a hydrogen bond which does not supply the bridging hydrogen atom

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83
Q

amino group

A

nitrogen atom bonded to two hydrogen atoms

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84
Q

hydroxyl group

A

-OH

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85
Q

phosphate group

A

phosphorus atom bonded to four oxygen atoms

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86
Q

weak acids

A

weak acid with the lower pH will dissociate to a greater extent in water than the other acid

87
Q

effective buffering range

A

+/- 1 of the pKa

ex: if the pKa = 6.5 and the effective buffering range is pH 5.5 to pH 7.5

88
Q

at physiological pH, the carboxylic acid group of an amino acid will be _____, while the amino group will be _____, yielding the zwitterion form

A

deprotonated, protonated

89
Q

what happens when proteins fold into their native conformation?

A

most of the non-polar, hydrophobic amino acid residues are found buried in the protein core

most of the polar, charged, and hydrophilic residues are found on the exterior surface of the protein

proteins adopt their lowest energy state form

90
Q

secondary protein

A

folded regions stabilized by backbone hydrogen bonding

91
Q

primary protein

A

sequence of amino acids

92
Q

quaternary protien

A

association of several protein chains

93
Q

tertiary protein

A

three-dimensional shape of the protein stabilized by side chain interactions

94
Q

the amino acid side chain residues in an alpha helix point _____ from the center of the helix

A

outward

95
Q

motifs and domains of proteins

A

separate proteins with similar domains are likely to have similar functions

96
Q

what structure does myoglobin have?

A

tertiary

97
Q

lyase

A

can catalyze reactions that link two compounds together through the formation of a new chemical bond and without the use of water

98
Q

Km in the Michaelis-Menten equation

A

equal to the [S] (substrate concentration) required to achieve 1/2 Vmax

99
Q

on a lineweaver-burk plot, what does the x-intercept represent?

A

-1/Km

100
Q

transferase

A

catalyze the transfer of groups among substrates

101
Q

isomerase

A

catalyze conversion between isomers

102
Q

oxidoreductase

A

catalyze redox reactions

103
Q

hydrolase

A

catalyze hydrolysis reactions

104
Q

ligase

A

catalyze synthesis reactions between substrates

105
Q

deltaG of a spontaneous reaction is…

A

< 0

106
Q

how do enzymes speed up reactions?

A

they lower the activation energy of the reaction

107
Q

as Km increases, the measured affinity of an enzyme for its substrate will…

A

decrease

108
Q

what rate constant is negligible when measuring the initial velocity of an enzyme-catalyzed reaction?

A

k-2

109
Q

ideal enzyme characteristics

A

small Km and large kcat

110
Q

what amino acid performs the nucleophilic attack in the chymotrypsin mechanism?

A

Ser

111
Q

the binding of a competitive inhibitor to an enzyme will cause the Vmax to _____ and the apparent Km to _____

A

remain unchanged, increase

112
Q

in hemoglobin, the heme group is _____ when oxygen is bound

A

planar

113
Q

competitive inhibitor

A

reversible inhibitor that binds the active site

114
Q

how do uncompetitive inhibitors alter the kinetics of an enzyme-catalyzed reaction?

A

decreased Vmax and decreased Km

115
Q

chymotrypsin mechanism (general)

A

deprotonation of Ser by His

nucleophilic attack by Ser

cleavage of peptide bond

deprotonation of water by His

Ser acts as leaving group and is cleaved from peptide fragment

diffusion of peptide fragment out of active site

116
Q

how does the oxyanion hole stabilize the tetrahedral intermediate?

A

hydrogen bonding with the backbone of the peptide chain

117
Q

myoglobin characteristics

A

acts as oxygen storage in tissue

has a higher affinity for oxygen than hemoglobin

118
Q

hemoglobin characteristics

A

acts as an oxygen transporter in the blood

exhibits cooperativity

has quaternary structure

119
Q

positive hemoglobin effectors

A

carbon monoxide

oxygen

120
Q

negative hemoglobin effectors

A

2,3-BPD

carbon dioxide

hydrogen ions

121
Q

according to the bohr effect, as the concentration of carbon dioxide increases, the concentration of H+…

A

increases

122
Q

the oxygen binding curve for fetal hemoglobin lays ______ adult hemoglobin

A

to the left of

123
Q

what molecules can form hydrogen bonds?

A

nitrogen, oxygen, or fluorine in the form of covalent compounds

124
Q

substitution of leucine for which of the following amino acids would be least likely to have an observable effect on the activity and structure of a protein?:

valine

arginine

tryptophan

glutamic acid

A

valine

125
Q

enzymatic catalysts affect ______ of a chemical reaction

A

only the rate

126
Q

michaelis-menten equation

A

Vo = Vmax*[S] / (Km + [S])

127
Q

what exerts its effects on hemoglobin by forming a carbamate ion when combined with the N-terminus of the globin chains?

A

CO2 (carbon dioxide)

128
Q

what amino acid increases the basicity of His in the catalytic triad of chymotrypsin?

A

Asp

129
Q

based on the mechanism of chymotrypsin, it would best be categorized as which class of enzyme?

A

hydrolase

130
Q

globular protein that performs its biological function as a single independent polypeptide chain

A

myoglobin

its tertiary structure is stabilized by the interactions of amino acid side chains in non-neighboring regions of the polypeptide chain

it could contain α-helices that are stabilized by hydrogen bonding

non-covalent forces are the primary source of stability for the secondary and tertiary structure

131
Q

tyrosine and tryptophan are less hydrophobic when compared to phenylalanine because…

A

phenylalanine lacks a polar group in its side chain

132
Q

kcat

A

represents the turnover number

can be calculated by Vmax/[E]total

133
Q

which of the following statements best describes the thermodynamics of protein folding as it nears its native state?

A

protein folding is primarily driven by the aggregation of hydrophobic residues in an aqueous solution

134
Q

a research study finds that inducing severely low blood phosphate levels in rats decreases the release of oxygen from the hemoglobin in red blood cells (RBC) to their tissues. which of the following conditions will most likely cause the same physiologic effect on hemoglobin oxygen release as seen in the study?

A

exposure to carbon monoxide

135
Q

in hemoglobin, the ________ stabilizes oxygen when it is bound and protects the iron from oxidation in the absence of oxygen

A

distal histidine

136
Q

substitution of which amino acids for Gly and Ser in the oxyanion hole of chymotrypsin would preserve the function of the oxyanion hole? ignore any changes to the overall structure and folding of the protein that may be caused by substitutions

A

any amino acid may be substituted

137
Q

slope of a lineweaver-burk plot

A

Km/Vmax

138
Q

the interior of an alpha helix contains ________________

A

atoms from the protein backbone in close contact

139
Q

anomeric carbon

A

the one with the double bond to oxygen and next to the carbon that is next to the end -OH

140
Q

triacylglycerol formation

A

droplets

141
Q

carbohydrate definition

A

1 carbonyl group and 2 hydroxyl groups

142
Q

enantiomers

A

nonsuperimposable mirror images

143
Q

alpha linolenic acid

A

humans can convert this into EPA and DHA; ALA is essential because we cannot synthesize it

144
Q

saturated fatty acids

A

solidifies easily, relatively high melting temperature

dispersion forces occur in nonpolar condensed form

need electron clouds to be close in space to get dispersion forces

145
Q

what types of bonds exist in glycogen?

A

alpha 1-4 and 1-6 bonds only

146
Q

anomers

A

subtype of diastereomers that differ at a new asymmetric carbon atom formed on ring closure (anomeric carbon)

147
Q

glucose is a _______ sugar

A

reducing

148
Q

proteoglycans

A

polysaccharide w/ small protein core that is covalently linked with N or O glycosidic bonds (around 5% protein)

149
Q

how is deoxyribose different from ribose?

A

deoxyribose has one less oxygen atom

150
Q

wax

A

long chain fatty acid esterified to long chain alcohol

151
Q

what factors determine the melting point of fatty acids?

A

the number of double bonds (sites of unsaturation)

152
Q

free fatty acid formation

A

micelle

153
Q

phospholipid formation

A

phospholipid bilayer; bilayer formation is largely driven by the hydrophobic effect

154
Q

isomers

A

same molecular formula but different structures

155
Q

constitutional isomers

A

differ in the order of attachment of atoms

156
Q

stereoisomers

A

atoms are connected in the same order but differ in spatial arrangement

157
Q

diastereomers

A

isomers that are not mirror images

158
Q

epimers

A

subtype of diastereomers that differ at one of several asymmetric carbon atoms

159
Q

anomeric carbon

A

the new chiral center formed in ring closure; it was the carbon containing the carbonyl in the straight-chain form; ether linkage

only ring carbon covalently attached to 2 oxygen atoms

160
Q

pyranose

A

carbohydrates that have a chemical structure that includes a six-membered ring system consisting of five carbon atoms and one oxygen atom

161
Q

furanose

A

carbohydrates that have a chemical structure that includes a five-membered ring system consisting of four carbon atoms and one oxygen atom

162
Q

alpha form

A

hydroxyl at C-1 is below the plane of the ring

163
Q

beta form

A

the hydroxyl at C-1 is above the plane of the ring

164
Q

glycosidic bond

A

linkage between monomer units

165
Q

O-glycosidic bond

A

bond formed between the anomeric carbon atom and a hydroxyl group of another molecule

166
Q

N-glycosidic bond

A

bond formed between the anomeric carbon atom and an amine

167
Q

what kind of bond do carbohydrates form with phosphates?

A

ester linkages

168
Q

fucose

A

one of few biological molecules active in the L-state

common to add on to obtain new properties due to its interesting structure

169
Q

glycoproteins

A

mostly protein

examples: antibodies or membrane proteins w/ bound oligosaccharides for some kind of cell-cell signal

170
Q

mucins

A

glycoprotein that is about 1/2 protein and polysaccharide

171
Q

how are carbohydrates attached in all glycoproteins?

A

attached to the nitrogen atom in the side chain of Asn (N-linkage) or to the oxygen atom of the side chain of Ser or Thr (O-linkage)

172
Q

fatty acid nomenclature

A

18:3(delta^9,12,15)

18: number of carbons
3: number of double bonds (unsaturated sites)
9, 12, 15: carbons where double bonds are; start count at C-1 (anomeric carbon)

173
Q

omega nomenclature

A

18:3(omega^1,3,6)

18: number of carbons
3: number of double bonds (unsaturated sites)
1, 3, 6: carbons where double bonds are; start count at end of carbon chain (opposite C-1)

174
Q

unsaturated fatty acids

A

acyl chains are liquid and solidify at relatively low temperature

no/low dispersion forces so cannot pack tightly together

175
Q

triacylglyerol

A

storage form of energy

typically saturated but can be unsaturated

glycerol + 3 fatty acids

176
Q

glycerol

A

three-carbon alcohol to which fatty acids are covalently bonded to make fats

177
Q

why are triacylglycerols contained in adipocytes?

A

free fatty acids are charged and need a safe way to be stored

simple hydrolysis/dehydration is used to store molecules

178
Q

phospholipid components

A

fatty acids (2+), a platform, a phosphate, and an alcohol

platforms: glycerol or sphingosine

179
Q

sphingosine

A

palmitate + serine

backbone: CH - CH - CH2

head group: OH

amine group: site of attachment for the fatty acid that will get swapped out

180
Q

cholesterol

A

most common steroid that plays a role in maintaining membrane fluidity

181
Q

structure of steroids

A

3 cyclohexane rings and 1 cyclopentane ring

182
Q

transverse diffusion

A

outer to inner layer; flip-flop, very slow, requires enzyme (flipases)

183
Q

lateral diffusion

A

movement within the same layer; rapid

184
Q

integral membrane protein

A

can be used for signaling; extends through all or part of membrane/can form a tunnel

tend to have a higher concentration of hydrophobic amino acids on their surface

185
Q

peripheral membrane protein

A

attaches only at surface of the membrane

anchored proteins can exist (anchored via lipid and covalent bond)

can move hydrophobic molecules to active site

186
Q

nonmediated transport

A

no special protein needed to complete

rapid: hydrophobic (lipophilic) solutes
slower: polar/charged solutes (membranes are effective barriers to the diffusion of polar/charged molecules)

diffuses CO2 and O2

187
Q

facilitated (passive) transport

A

does not require energy other than the concentration gradient; diffusion of certain solutes is accelerated by specific transporter proteins

pore, channel, carrier

188
Q

facilitated (active) transport

A

transporter proteins that achieve transport against a concentration gradient

189
Q

uniport

A

membrane transport process that carries one type of solute

190
Q

symport

A

membrane transport process that carries two substances in the same direction across the membrane

typically, one species moves with the gradient and another moves against it (accounts for energy balance)

191
Q

antiport

A

membrane transport process that carries one substance in one direction and another in the opposite direction

ex: Na+ and Ca2+ // Na+ moves with the gradient and causes structural change which causes Ca2+ to move against its gradient

192
Q

pump

A

moving against the gradient

ex: sodium-potassium pump; energy of hydrolysis of ATP pushes energy

193
Q

channel

A

first entry is large enough for the solute + hydrogen sphere to enter

selectivity filter: water molecules are forced to shed and the carbonyl oxygens of the polypeptide are at the right geometry and distance to cause a bond and polar attraction to potassium

194
Q

how do channels become specific for certain ions?

A

channel narrows to prevent large ions from passing through

ions that are too small are unable to interact with the selectivity filter backbone carbonyl groups in the protein, meaning they cannot shed their hydration shell

when the specific ion passes through, it replaces its hydration interactions with those of the peptide carbonyls

195
Q

glycosaminoglycan

A

composed of repeating units of a disaccharide: one is a derivative of an amino sugar and the other carries a negative charge (ex: carboxylate or sulfate)

196
Q

how does negative charge contribute to glycosaminoglycan structure?

A

negative charge can be used to pull water into the tissue (ex: cartilage), allowing for tissue to withstand compressive forces and sustain tension to become flexible

197
Q

flow of K+ ions out of the cell through channels is…

A

spontaneous

198
Q

transport of K+ ions into the cell via pump is…

A

non-spontaneous

199
Q

formula for simple carbohydrate

A

Cn(H2O)n

ex: C6H12O6

200
Q

when numbering carbons…

A

start from the end that will give the carbonyl the lowest number

201
Q

hemiacetal

A

alcohol + aldehyde (R-CH=O)

202
Q

hemiketal

A

alcohol + ketone (R2-C=O)

203
Q

reducing end

A

the end of a chain with a free anomeric carbon

signaled by hemiacetal or hemiketal

204
Q

function of triacylglycerols in animals include

A

storage for long-term energy and thermal insulation of body temperature

205
Q

glycerol and fatty acid linkage

A

ester linkage

206
Q

fluidity of a bilayer is generally increased by…

A

an increase in the number of double bonds in the fatty acid hydrocarbon chains

207
Q

membranes are a fluid mosaic of what components?

A

phospholipids, proteins, and cholesterol

208
Q

in the hydrophobic environment of a membrane, the alpha helix of a protein folds such that the outer surfaces contain mostly ________ amino acids, while _______ amino acids are mostly buried on the inside

A

non-polar on outside
hydrophilic on inside

209
Q

the most _______ molecules will be the most permeable

A

hydrophobic

210
Q

phosphatidate

A

glycerol-3 phosphate and two fatty acid chains

211
Q

acetal

A

functional group that contains a carbon atom bonded to two -OR groups, an alkyl chain, a hydrogen atom

212
Q

ketal

A

functional group that contains a carbon atom bonded to two -OR groups and two alkyl chains

213
Q

fatty chain length’s relation to melting point

A

longer chains can withstand higher temps

shorter chain can withstand cooler temps

UT BCH 369 (2 decks)

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