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OLD "MBS 602" > Exam 1 > Flashcards

Exam 1 Flashcards

1
Q

What are the two functional groups of amino acids?

A

amino (NH2)
carboxyl (COOH)

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2
Q

What does an amino acid backbone look like?

A

NH2–C(alpha)–COOH

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3
Q

Amino acids contain a central __________ carbon atom

A

tetrahedral

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4
Q

Only ____-amino acids are found in eukaryotes

A

L

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5
Q

What is the only amino acid in eukaryotes that isn’t in the L conformation and why?

A

glycine
its R group is just an H

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6
Q

Are water molecules charged are neutral?

A

neutral

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7
Q

Are water molecules polar or non-polar?

A

polar

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8
Q

What is the strongest bond?

A

covalent

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9
Q

Why does NaCl dissolve easily in water?

A

its very positive so it makes bonds with water easily

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10
Q

Are polar or non polar molecules insoluble?

A

nonpolar

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11
Q

What makes aspartic acid and glutamic acid polar negative?

A

carbonyl R groups

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12
Q

What makes lysine, arginine, and histidine polar positive?

A

amine R groups

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13
Q

What makes asparagine and glutamine polar uncharged?

A

Amine R group

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14
Q

What makes serine, threonine, and tyrosine polar uncharged?

A

OH R groups

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15
Q

What makes glycine, alanine, valine, leucine, and isoleucine nonpolar?

A

carbonyl R groups

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16
Q

What rare amino acid is considered the 21st amino acid and is used as a stop codon?

A

Selenocysteine (SEC, U)

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17
Q

Where is the rare amino acid hydroxylysine and hydroxproline usually found?

A

connective tissue (collagen)

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18
Q

Where is the rare amino acid carboxyglutamic acid usually found?

A

clotting factors

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19
Q

What rare amino acid is found in bacteria?

A

PCA (pyroglutamic acid)

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20
Q

What is the role of amino acid that do not occur in proteins?

A

neurotransmitters and hormones

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21
Q

What are essential amino acids?

A

received through the diet (humans cannot synthesize)

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22
Q

What are conditionally essential amino acids?

A

made under times of stress

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23
Q

What are dispensable amino acids?

A

easily made all the time

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24
Q

Amino acids are amphoteric, what does this mean?

A

they can either accept a proton or donate a proton

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25
Q

What does the cationic form an amino acid look like?

A

NH3+
COOH

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26
Q

What does the zwitterion form an amino acid look like?

A

NH3+
COO-

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27
Q

What does the anionic form an amino acid look like?

A

NH2
COO-

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28
Q

How do you calculate isoelectric point of a molecule?

A

PI = pK1 + pK2 / 2

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29
Q

What is the isoelectric point?

A

the pH at which a molecule is electrically neutral

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30
Q

How many pKa does a charged amino acid have?

A

3

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31
Q

Does formation of a peptide bond cause dehydration and rehydration?

A

dehydration

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32
Q

How does a peptide bond come together?

A

COO- bonds with NH2

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33
Q

What enzyme catalyzes peptide bond formation?

A

peptidyl transferase

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34
Q

What conformation are peptide bonds in?

A

trans

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35
Q

Is the peptide bond fully or partial double bonded?

A

partial

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36
Q

What is the length of a peptide bond?

A

0.133 nm

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37
Q

Due to the double bond characteristics, the peptide bond is on a ________ plane

A

amide

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38
Q

What direction is the protein read in?

A

N to C terminus

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39
Q

What level of protein structure is primarily determined by hydrophobic/phillic interactions?

A

tertiary

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40
Q

What are 2 ways proteins can be sequenced?

A
  1. real amino acid sequencing
  2. sequencing the corresponding DNA in the gene
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41
Q

What are 2 examples of real amino acid sequencing?

A

Sanger method
Mass spec

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42
Q

Protein function depends on _________

A

structure

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43
Q

Protein structure depends on sequence and ___________ forces

A

non-covalent

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44
Q

Is the number of protein folding patterns infinite or finite?

A

finite

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45
Q

Marginal stability facilitates ________

A

motion

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46
Q

Motion enables ___________

A

function

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47
Q

What bond is Phi and Psi inbetween?

A

Phi: C(a)–N
Psi: C(a)–C(o)

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48
Q

What are the possible phi and psi angles?

A

anything but 0

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49
Q

Secondary, tertiary, and quaternary structure of protein is formed and stabilized by ___________

A

non-covalent forces

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50
Q

Where do ionic interactions usually occur on a protein?

A

surface

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51
Q

Hydrogen bonding between ____ and ____ on peptide backbone is common

A

C=O
NH

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52
Q

Secondary protein structure is primarily stabilized by ___________

A

hydrogen bonds

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53
Q

What are 4 examples of secondary protein structure?

A

alpha helix
other helix
beta sheets
beta turns

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54
Q

What are alpha helices stabilized by?

A

hydrogen bonds

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55
Q

What is a dipole moment?

A

arrangment of NH groups are pointed one way and C=O groups are pointed in same the other making one end positive and one end negative (alpha helix)

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56
Q

What is helical capping?

A

Formation of H bonds with other nearby donors at the end of helicies

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57
Q

What is a anphiphilic helix?

A

hydrophobic lines up on one side and hydrophilic on the other

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58
Q

What holds beta pleated sheets together?

A

hydrogen bonds

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59
Q

How many residues are required for a beta turn?

A

4

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60
Q

What 2 amino acids are common in beta turns?

A

proline
glycine

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61
Q

What amino acid is never found in the middle of an alpha helix or beta sheet because it causes a kink/turn in peptide chain?

A

proline (has a large ring)

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62
Q

What is Type I beta turn?

A

proline in position 3

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63
Q

What is Type II beta turn?

A

proline in position 2
glycine in position 3

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64
Q

What is the cause of Sickle Cell Anemia?

A

Glu to Val (single base change)

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65
Q

Why do protein secondary structures form whenever possible?

A

hydrogen bonding

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66
Q

What two ways do proteins fold to be more stable?

A

formation of intramolecular bonds
reduction in the surface area

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67
Q

What is the only covalent bonding in protein folding?

A

disulfide bonds

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68
Q

Globular or fibrous? Create maximum internal bonds (intramolecular) and minimize solvent contact

A

globular

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69
Q

Globular or fibrous? Create maximum intermolecular bonds and maximize molecule to molecule contact

A

fibrous

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70
Q

Do all proteins have quaternary structure?

A

No (but they all have 1, 2, 3)

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71
Q

Covalent or non-covalent association for globular proteins?

A

non-covalent

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72
Q

Covalent or non-covalent association for fibrous proteins?

A

Covalent

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73
Q

What are the 5 advantages of quaternary structure?

A
  1. stability
  2. efficiency
  3. assembly
  4. cooperativity/allostery
  5. regulation
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74
Q

How do quaternary proteins have stability?

A

minimize surface area

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75
Q

How do quaternary proteins have efficiency?

A

synthesize large protein in small subunits

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76
Q

How do quaternary proteins have assembly?

A

combination of 2 proteins to make a catalytic site

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77
Q

How do quaternary proteins have cooperativity/allostery?

A

binding of one substrate increases affinity for other substrates

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78
Q

What is the simplest kind of symmetry?

A

rotational

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79
Q

Can quaternary structures polymerize?

A

yes

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80
Q

What are 3 examples of quaternary structures that can polymerize?

A

Tubulin
TMV
flagella

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81
Q

What are the 4 classes of globular proteins?

A

alpha
beta
alpha/beta (combined)
alpha+beta (seperate)

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82
Q

Are globular or fibrous proteins more common?

A

globular

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83
Q

In fibrous proteins, polypeptide chain is organized _______ to a single axis

A

parallel

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84
Q

What is alpha keratin made of?
What is beta keratin made of?

A

alpha keratin: alpha helix
beta keratin: beta sheets

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85
Q

Are fibrous proteins soluble or insoluble?

A

insoluble

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85
Q

What are 3 examples of fibrous proteins?

A

alpha keratin
beta keratin
collagen

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86
Q

What is the amino acids sequence for beta keratin?

A

Gly—–Ala/Ser—-Gly——-Ala/Ser………
every other amino acid is a glycine

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87
Q

What is beneficial about all the glycine’s in beta keratin pointed the same way?

A

allows for tight packing of sheets

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88
Q

alpha keratin is what shape?

A

coiled coil

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89
Q

What is a coiled coil?

A

dimers line up to form a antiparallel tetramer

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90
Q

Alpha keratin is 2 _____ alpha helices super coiled in a _____handed manner

A

2 right handed —> left handed

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91
Q

What is the defect in Osteogenesis imperfecta?

A

collagen

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92
Q

What is the defect in Creutzfeldt-Jacob disease?

A

prions (misfolded proteins)

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93
Q

What is the defect in Sickle Cell anemia (protein wise)?

A

polymerization of hemoglobin

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94
Q

What is the most abundant protein in animals?

A

collagen

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95
Q

What is the most common collagen type?

A

Type I

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96
Q

What is the amino acids sequence for collagen?

A

Gly——X——-Y
X = proline
Y = hydroxyproline

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97
Q

What are the 2 modified amino acids found in collagen?

A

hydroxyproline
hydroxylysine

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98
Q

What is required for the hydroxylation of proline in collagen?

A

Proline
oxygen
alpha-ketogluterate
ascorbic acid (Vit C)

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99
Q

What are the products of hydroxylation of proline in collagen?

A

hydroxyproline
succinate
dehydroascrobate

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100
Q

How is scurvy caused?

A

deficiency in vitamin C causes no hydroxylation of proline affecting collagen

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101
Q

What is required for the hydroxylation of lysine in collagen?

A

lysine
oxygen
alpha ketogluterate
ascorbic acid (Vit C)

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102
Q

Attaching glucose to _____________ creates bone mineralization

A

5-hydroxylysine

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103
Q

What is the enzyme involved in hydroxylation of proline?

A

Prolyl hydroxlyase

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104
Q

What is the enzyme involved in hydroxylation of lysine?

A

lysyl hydroxylase

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105
Q

Collagen has high levels of glycine, proline, and hydroxyproline. How does this affect collagen’s secondary structure?

A

CANNOT form traditional alpha helices and beta sheets
-forms left handed helicies

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106
Q

What is the tertiary structure of collagen?

A

3 left handed helices intertwine to form a right handed triple helix

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107
Q

In the tertiary structure of collagen, every third residue is _________ which points inside the helix

A

Gly

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108
Q

What is tropocollagen?

A

basic structural unit of collagen (before individual collagen cross link together)

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109
Q

What occurs in the holes present when collagen cross links?

A

bone mineralization when glucose is added to hydroxylysine

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110
Q

What is Type I collagen called?

A

fiber forming

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111
Q

Where is most of the iron and heme in our bodies located?

A

RBC

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112
Q

As young cells differentiate into RBC, _____ continent increases

A

hemoglobin

113
Q

Gamma globin is is fetal or adult?

A

fetal

114
Q

Beta globin is fetal or adult?

A

adult

115
Q

Does gamma globin increase or decrease with age?

A

decrease (its fetal globin)

116
Q

Cooley’s anemia is caused by the absence of ___________ chains

A

beta globin

117
Q

Myoglobin is a monomeric oxygen ______ protein

A

storage

118
Q

Hemoglobin is a tetrameric oxygen __________ protein

A

transport

119
Q

Hemoglobin is an allosteric _________

A

regulator

120
Q

_______ iron interacts with 6 ligands in Hb and Mb

A

heme

121
Q

When Mb or Hb bind oxygen, the O2 molecule binds to ____________

A

heme iron

122
Q

What happens when O2 binds to the heme iron as the last ligand?

A

the heme plane is tilted (conformational change) rupturing the salt bridges

123
Q

How many binding ligands does Hb or Mb?

A

6

124
Q

DeoxyHb is the tense or relaxed state?
and is O2 bound?

A

tense
O2 not bound

125
Q

OxyHb is the tense or relaxed state?
and is O2 bound?

A

relaxed
O2 bound

126
Q

The oxygen binding curve for Mb and Hb is what shape?

A

Mb:hyperbolic
Hb: sigmoidal

127
Q

what is the effect of the oxygen binding curve for Hb being sigmoidal shaped?

A

positive cooperativity

128
Q

What is the positive cooperativity effect on the oxygen binding curve?

A

When the first oxygen binds it easier for the other oxygens to bind

129
Q

What is the P50 on an oxygen binding curve?

A

partial pressure of oxygen when Hb is 50% saturated

130
Q

P50 is ________ proportional to the oxygen affinity

A

inversely

131
Q

Does Hb or Mb have a greater affinity for oxygen at all presures?

A

Mb

132
Q

Hb binds to oxygen in the _______ and releases it in the capillaries

A

lungs

133
Q

What is 2,3-bisphosphoglycerate?

A

allosteric effector of hemoglobin

134
Q

The sigmodial binding curve shape is only observed in the presence of _____________

A

2,3-bisphosphoglycerate

135
Q

_____________ binds at a site distant from Fe where oxygen binds, which makes it an allosteric effector

A

2,3-bisphosphoglycerate

136
Q

Why does 2,3-bisphosphoglycerate bind easily to Hb?

A

its very negative and Hb is very positive

137
Q

What is the purpose of 2,3-bisphosphoglycerate?

A

stabilizes deoxyHb (tense form;no oxygen bound)
- allows the hemoglobin to act as an effective oxygen carrier delivering oxygen to muscles

138
Q

Fetal hemoglobin has a higher affinity for O2, why?

A

because it has a lower affinity for 2,3-bisphosphoglycerate (2,3-BPG stabilizes oxygen off loading)

139
Q

Where is the fetal Hb located on the oxygen saturation curve?

A

to the left because it has high oxygen affinity because it doesn’t bind well to 2,3-bisphosphoglycerate

140
Q

What is the mechanism of sickle cell anemia involving hemoglobin?

A

when Hb goes deoxy (no O2 bound), a pocket is exposed causing Hb to polymerize and distort shape

141
Q

What is the new CRISPR study for Sickle Cell Anemia?

A

decrease BCL11A which suppresses fetal hemoglobin

142
Q

Water has ________ specific heat

A

high

143
Q

Water has __________ fusion and vapor heat

A

high

144
Q

Water has ___________ surface tension

A

high

145
Q

Is water polar or non-polar?

A

polar

146
Q

How many H bonds can water form?

A

4

147
Q

Why does water have a dipole moment?

A

The O makes one side negative and Hs make the other side positive

148
Q

How many hydrogen bonds does water and ice make?

A

ice: 4
water: 2.3

149
Q

Is water or ice more stable half life?

A

ice

150
Q

Is ice or water less dense?

A

ice

151
Q

What is capillary action of water?

A

water rises in narrow tubes against gravity

152
Q

Why is ice less dense than water?

A

it forms a lattice shape where the molecules are more spread out

153
Q

What is important about water having a high dielectric constant?

A

dissolve ions easily

154
Q

What is a hydration shell?

A

water surrounds ions (positive ions have oxygen pointing towards them)

155
Q

What are colligative properties?

A

physical changes that occur when a solute is added to a solvent (water)

156
Q

What are the 4 colligative properties of water?

A
  1. vapor pressure lowering
  2. boiling point elevation
  3. freezing point depression
  4. increased osmotic pressure
157
Q

Explain water having increased osmotic pressure when a solute is added

A

when solute is added to water it rises in semipermeable tube and 1 atm needs to be added to lower the level to before

158
Q

How do nonpolar solutes organize water?

A

The H bonds reorganize water

159
Q

Does non-polar solutes increase or decrease entropy?

A

decrease (less chaos)

160
Q

What is an amphiphilic molecule?

A

attracted to both polar and nonpolar environments

161
Q

What is an amphipathic molecule?

A

contain both polar and nonpolar group

162
Q

What is an example of an amphipathic molecule?

A

fatty acids

163
Q

What does ionized water form?

A

hydronium ions (H3O or H+)

164
Q

What is the equation for Ka?

A

Ka = [H+][A-]/[HA]

165
Q

Ka = [H+][A-]/[HA]
What is the HA?

A

weak acid

166
Q

Ka = [H+][A-]/[HA]
What is the A-?

A

conjugate base

167
Q

What is pKa?

A

When weak acid is 50% acid and 50% base

168
Q

On a titration curve, what happens when the pH is close to the pKa?

A

the pH barley changes

169
Q

When pKa is 0.5 then its equal to the ____

A

pH

170
Q

How do you determine how many humps are there on a titration curve?

A

how many hydrogens the molecules have

171
Q

What are buffers?

A

solutions that resist changes in pH as acids or bases are added

172
Q

Buffers can only be used reliably within a pH of ____ from thier pKa

A

1

173
Q

What is Gibbs free energy (G)?

A

amount of usable energy in that system to do work

174
Q

What is the equation for Gibbs free energy?

A

G=H-TS

175
Q

What is H?
What is S?
in Gibbs free energy

A

H = enthalpy (heat)
S = entropy (disorder)

176
Q

Is a positive delta G an endergonic or exergonic reaction?

A

endergonic

177
Q

Is a positive delta G a spontaneous or non-spontaneous reaction?

A

non-spontaneous

178
Q

endergonic = spontaneous or non-spontaneous reaction?

A

non-spontaneous

179
Q

Is a negative delta G an endergonic or exergonic reaction?

A

exergonic

180
Q

Is a negative delta G a spontaneous or non-spontaneous reaction?

A

spontaneous

181
Q

exergonic = spontaneous or non-spontaneous reaction?

A

spontaneous

182
Q

Which direction does the arrow go for endergonic reactions?

A

backwards

183
Q

Which direction does the arrow go for exergonic reactions?

A

forward

184
Q

For endergonic reaction, Does the initial G or final G higher energy?

A

G final (goes from lower to higher energy)

185
Q

For exergonic reaction, Does the initial G or final G higher energy?

A

G initial (goes from higher to lower energy)

186
Q

Do exergonic or endergonic reactions release energy?

A

exergonic

187
Q

Do exergonic or endergonic reactions require energy?

A

endergonic

188
Q

Endergonic reactions are usually what kind of reactions?

A

synthesis

189
Q

Exergonic reactions are usually what type of reactions?

A

break down

190
Q

What does the little circle next to the delta G mean?

A

standard gibbs free energy (same constants)

191
Q

How are endergonic reactions possible in the body even though they are not favored because they require energy?

A

energy coupling (ex ATP)

192
Q

What are the 3 chemical groups of ATP?

A

three phosphates
adenine
ribose

193
Q

What is the order of the three phosphates on ATP?

A

gamma (business end)
beta (middle)
alpha (next to ribose)

194
Q

Is ATP hydrolysis spontaneous or non-spontaneous?

A

spontaneous

195
Q

What is the non-native structure of proteins?

A

unfolded (primary structure)

196
Q

What is a native structure of a protein?

A

folded conformation

197
Q

Is protein folding spontaneous or non-spontaneous?

A

spontaneous

198
Q

If protein folding is spontaneous, what is the gibbs free energy and is the starting energy higher or lower?

A

negative G
starting E is higher

199
Q

When G is negative, what is H and S?

A

H < 0 (releasing heat)
S > 0 (environment around protein is now disordered)

200
Q

Electrostatic interactions occur between _______ and ________

A

cation and anion

201
Q

What 3 things are needed for an H bond?

A
  1. acceptor
  2. donor
  3. hydrogen
202
Q

What is the most common acceptor and donor in H-bonds?

A

acceptor: oxygen
donor: nitrogen

203
Q

What happens in van der Waal interactions if the molecules atomic volumes get too close?

A

they aren’t attracted anymore and are repulsed from each other

204
Q

Hydrophobic effect is not an attractive force, its a ______________ driven process

A

thermodynamically driven

205
Q

What is the value of water being able to shield?

A

weaken interactions between molecules

206
Q

What are the 4 trivial enzyme names?

A

kinase
phosphate
dehydrogenase
reductase

207
Q

What are zymogen enzymes?

A

inactive precursor of an enzyme that has little or no enzymatic activity
but once proceed post-translationally it become active

208
Q

What are coenzymes?

A

non-peptidic molecules that bind to enzyme and are needed for reaction to take place

209
Q

____ are not refereed to as coenzymes

A

ions

210
Q

What are cofactors?

A

same as coenzymes but are substrates of low abundance (ex NAD+)
-typically a chemical group
- not required

211
Q

What are prosthetic groups?

A

cofactors that are tightly/covalently bound to enzyme

212
Q

What are apoenzymes?

A

(typically inactive) coenzyme-dependent enzyme that doesn’t have the co-enzyme bound to it

213
Q

What is a holoenzyme?

A

when the Apoenzyme has the coenzyme bound to it (active)

214
Q

What are isoenzymes?

A

enzymes that catalyze the same reaction yet differ in thier amino acid sequence (hexokinase)

215
Q

Isoenzyme catalyze the same reactions but have different ______ and ____

A

Vmax
Km

216
Q

Why don’t spontaneous reactions just occur all the time in a cell?

A

it must get past the activation energy barrier

217
Q

What helps a reaction get over the activation energy by lowering it?

A

enzymes

218
Q

Enzymes only affect the reaction path not the ______ and _______

A

products and reactants

219
Q

Most enzymes in a cell are proteinaceous, what does proteinaceous mean?

A

built by amino acids and cofactors

220
Q

What is the worlds oldest and most abundant enzyme?

A

ribozyme (RNA)

221
Q

What is enzyme specificity?

A

an enzyme has an active site SPECIFIC for a given substrate

222
Q

What is the Lock and Key theory?

A

substrate fits into enzyme like a key in a lock

223
Q

Why is the lock and key theory not completely correct?

A

enzymes can change to fit their substate

224
Q

What is the Induced fit theory?

A

enzymes can change to fit their substate

225
Q

What is the catalytic constant (kcat)?

A

the rate of ES –> E + P (cannot be reversed)
slowest step of reaction

226
Q

kcat is also known as the turnover number, what does that mean?

A

maximal number of catalytic cycles an enzymes performs in one second (similar to RPM)

227
Q

How do you calculate the turnover number (kcat)?

A

1/duration of catalytic cycle

228
Q

What is the unit of measurement of kcat?

A

s-1

229
Q

According to Michaelis-Menten kinetics…
The [E] is much _________ than [S]

A

smaller

230
Q

According to Michaelis-Menten kinetics…
[E] and [S] binding is ________ and defined by k1 and k-1

A

reversible

231
Q

According to Michaelis-Menten kinetics…
formation of product is _____________

A

irreversible

232
Q

According to Michaelis-Menten kinetics…
What is the steady state assumption?

A

the [ES] is constant during the initial peroid of enzyme reaction
as the [ES] forms = slowing of [ES] formation rate

  • number of people entering and exiting the room is the same
233
Q

What is the Michaelis-Menten kinetics equasion for v/Vmax?

A

v/Vmax = [S] / Km+[S]

234
Q

0

A

0

235
Q

Why is the v/Vmax and [S] curve hyperbolic for affinity?

A

as the [S] starts increasing the rate us very fast but as more S is added the enzymes slows down

236
Q

How do you find Km on graph?

A

go to 0.5 on the Y axis and go down

237
Q

What does Km indicate?

A

how well the enzyme interacts with the substrate (AFFINITY)

238
Q

Is a higher or lower Km mean a stronger affinity for substrate?

A

lower Km (more left on curve)

239
Q

When [S] > Km the v/Vmax = ?

A

1 ( aka v=Vmax)
-cannot go any faster

240
Q

As Km increases, [S] __________

A

increases

241
Q

How do you make an enzyme reach Vmax?

A

add more substrate

242
Q

Michaelis-Menten kinetics only applies to what kind of enzymes?

A

ones with 1 active site

243
Q

What is cooperativity?

A

when first substrate binds enhances the binding of other substrates

244
Q

What is the shape of cooperativity enzymes on a graph?

A

sigmoidal (S-shaped)

245
Q

How do you tell on a graph which enzyme has more cooperativity?

A

at concentrations below K0.5, the most cooperative line has low activity
at concentrations above K0.5, the most cooperative line has high activity

246
Q

When an enzyme has high cooperativity, its activity below Km (S 0.5) is very ______, but _________ after the [S] exceeds S 0.5

A

low
increases

247
Q

What is an allosteric site?

A

used by small molecules to bind to enzyme not at active site and inhibits or activates

248
Q

How does allosteric activators affect V max?

A

increases (enzyme can go faster)

249
Q

How does allosteric activators affect Km?

A

decrease
(much sharper curve increase)

250
Q

Where do competitive inhibitors bind?

A

active site

251
Q

non-competitive inhibitors are the same as _________ inhibitors

A

allosteric

252
Q

Who do you get rid of competitive inhibitors?

A

increase [S] and it will kick inhibitor out

253
Q

What are irreversible inhibitors?

A

bind covalently to active site
ex: aspirin

254
Q

What is inhibition of the activity of an enzyme by a downstream product?

A

feedback inhibition

255
Q

What is inhibition of an enzyme by its own product?

A

product inhibition

256
Q

What is downstream activation of an enzyme by a compound upstream in a pathway

A

feedforward activation

257
Q

Enzyme that catalyze __________ reactions are usually very regulated

A

irreversible

258
Q

What is flux in steady state?

A

concentration of reactants and products doesnt change (waterfall)

259
Q

If an enzyme is blocked (deficient) what happens
upstream…
downstream…
first irreversible reaction…

A

upstream - increased [ ]
downstream - decreased [ ]
first irreversible reaction - nothing

260
Q

What is the 2 equations for pH?

A

pH = -log[H+]

pH = pKa + log [A-]/[HA]

261
Q

How do you find the moles of a solute?
How do you find the concentration from that?

A

grams X 1 mol/grams

mol/volume

262
Q

How do you find the [H+] if found the [OH]?

A

10e-14 – [H+]

263
Q

If a enzyme has a small Km what does that mean for affinity?

A

the smaller the Km the stronger the affinity

264
Q

If an enzyme is slower at low concentrations then faster at higher concentrations, what does that say about the cooperativity?

A

it has high cooperativity because it is able to easily bind more substrate once some is bound

265
Q

What shape curve does cooperativity have? What shape does affintiy have?

A

cooperativity: sigmoidal
affinity: hyperbolic

266
Q

Are proteins more or less soluble at thier isoelectric point?

A

least soluble (neutrally charged)

267
Q

Does increasing Hb cooperativity promote unloading of O2?

A

No, increased Hb cooperativity helps O2 bind better to Hb

268
Q

Does increasing [CO2] promote unloading of O2?

A

yes

269
Q

Does increasing [2,3-BPG] promote unloading of O2?

A

yes

270
Q

Does fetal Hb have a higher or lower affinity for O2 and why?

A

high
because it has a low affinity for 2,3-BPG

271
Q

Dissolved solutes alter colligative properties of water because they change…

A

the concentration of water

272
Q

What must a buffer consist of?

A

weak acid and strong conjugate base

273
Q

What is the optimal van der Waal distance?

A

3.4 A

274
Q

At which point in an enzymatic reaction will the Michaelis constant (Km) equal substrate concentration?

A

V = 1/2Vmax

275
Q

How does a competitive inhibitor affect Vmax?

A

no effect
- as more S is added the inhibitor will just get kicked out so it wont affect speed at high [S]

276
Q

How does a competitive inhibitor affect Km?

A

increases Km
- since some of the active sites are occupied by the inhibitor, more S is needed to achieve the same level of activity

277
Q

How does a competitive inhibitor affect kcat?

A

no effect
- doesn’t affect Vmax so it does effect kcat

278
Q

How does a non-competitive inhibitor affect Vmax?

A

decrease Vmax
- inhibitor is always present since its not in the active site so it wont be kicked out

279
Q

How does a non-competitive inhibitor affect Km?

A

no effect
- The substrate can bind regardless of the inhibitor because its not bound to the active site, so substrate can easily bind as if the inhibitor isnt there

280
Q

How does a non-competitive inhibitor affect kcat?

A

decreases kcat
- decreases Vmax so it decreases kcat

OLD "MBS 602" (7 decks)

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