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Part 1 Boards > Part 1: Biochemistry (AA’s, DNA/RNA, Macromolecules) > Flashcards

Part 1: Biochemistry (AA’s, DNA/RNA, Macromolecules) Flashcards

1
Q

All amino acids exist in the L form except for

A

Glycine

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2
Q

Why is Glycine not in the L form?

A

It doesnt contain a chiral carbon

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3
Q

Chiral carbons have different…

A

Compounds at each binding site

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4
Q

All Amino Acids are _____________. (Can act as an acid or a base)

A

Amphoteric

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5
Q

Name all of the Essential Amino Acids: (10)

A

[PVT TIM HALL]
Phenylalanine
Valine
Tryptophan

Threonine
Isoleucine
Methionine

Histidine
Arginine
Leucine
Lysine

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6
Q

What amino acid is essential in a child but not an adult?

A

Histidine

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7
Q

What are the purely ketogenic amino acids?

A

Leucine & lysine

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8
Q

What amino acid is the precursor to carnitine?

A

Lysine

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9
Q

What molecule takes fatty acids into the mitochondria for B Oxidation?

A

Carnitine

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10
Q

What are the Aromatic Amino acids?

A

Phenylalanine, Tyrosine, Tryptophan

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11
Q

What aromatic amino acid has an indole ring?

A

Tryptophan

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12
Q

What amino acids contain sulfur?

A

Cysteine & Methionine

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13
Q

What are the branched chain amino acids?

A

Isoleucine
Leucine
Valine

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14
Q

What disease results from the inability to break down branched chained amino acids?

A

Maple syrup urine disease

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15
Q

What are the acidic amino acids?

A

Aspartate & Glutamate

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16
Q

What are the Basic (not acidic) amino acids?

A

Histidine
Lysine
Arginine

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17
Q

When do basic amino acids have the greatest positive net charge?

A

At normal blood pH

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18
Q

Protein source and its limiting amino acid: Wheat & rice

A

Lysine

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19
Q

Protein source and its limiting amino acid: Legumes

A

Tryptophan

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20
Q

Protein source and its limiting amino acid: Maize

A

Lysine & Tryptophan

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21
Q

Protein source and its limiting amino acid: Pulses

A

Methionine or Cysteine

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22
Q

Protein source and its limiting amino acid: Egg, Chicken

A

None

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23
Q

Phenylalanine is converted into…

A

Tyrosine

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24
Q

Deficiency of phenylalanine hydroxylase leads to ____________ meaning ______________.

A

Phenylketonuria (PKU); cant convert to tyrosine

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25
Q

Tyrosine is converted into…

A

L Dopa -> Dopamine -> Norepinephrine -> Epinephrine
OR
L Dopa -> Melanin
OR
T3, T4

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26
Q

What is the result of not being able to convert L Dopa to Melanin?

A

Albinism

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27
Q

Histidine is converted into…

A

Histamine

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28
Q

Tryptophan is converted into…

A

Serotonin -> melatonin
OR
Niacin -> Nicotinamide

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29
Q

For every ___ kg of body weight we need ___ g of protein.

A

10; 8

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30
Q

What does isoelectric point mean?

A

PH when an amino acid has no net electrical charge (neutral)

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31
Q

What does Zwitter Ion mean?

A

An amino acid at its isoelectric point

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32
Q

Glutathione = ___peptide of _________ + _________ + ____________.

A

Tri peptide; Glycine, Glutamate, Cysteine

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33
Q

What mineral is for the enzyme Glutathione Peroxidase?

A

Selenium

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34
Q

Example of polypeptide hormones:

A

Insulin & Glucagon

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35
Q

Examples of catecholamines:

A

Epinephrine, Norepinephrine & dopamine

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36
Q

Examples of steroids:

A

Testosterone, cortisol, estrogen, progesterone

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37
Q

A peptide bone is a type of _______ bond that is…

A

Amide; specific for all proteins

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38
Q

Primary protein structure characteristics:

A

Linear sequence of amino acids

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39
Q

Secondary protein structure characteristics:

A

Alpha helices & beta pleated sheets both held together by hydrogen bonds

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40
Q

Examples of a secondary protein structure (3)

A

1) fibrous protein’s collagen
2) silk
3) 2 DNA strands together

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41
Q

Tertiary protein structure characteristics:

A

Contains disulfide bond & folding of single polypeptide chain in solution

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42
Q

What is the classic example of a tertiary protein structure?

A

Myoglobin

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43
Q

Quaternary protein structure characteristics:

A

2 or more polypeptide chains to make a functional protein & contains Hydrogen and Disulfide bonds

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44
Q

What is the classic example of a quaternary protein structure?

A

Hemoglobin

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45
Q

Enzymes act on the…

A

Substrate

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46
Q

Enzymes _______ rate of a reaction by _____________________.

A

Increase; lowering the activation energy

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47
Q

All enzymes are considered…

A

Catalysts

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48
Q

Km is a measure of what?

A

The affinity that an enzyme has toward the substrate

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49
Q

Km and Affinity have an ___________ relationship, therefore…

A

Inverse; if you increase Km affinity decreases

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50
Q

What is Vmax?

A

The max velocity of an enzyme

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51
Q

What is the equation for Km?

A

Km = 1/2 Vmax

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52
Q

What are the 3 major factors that affect the reaction velocity of an enzyme?

A

1) Substrate concentration
2) Temperature
3) pH

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53
Q

Km is the amount of ___________ required to reach __________.

A

Substrate; 1/2 Vmax

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54
Q

What is the effect of competitive inhibitors on Km and Vmax?

A

Km: increases
Vmax: does not change

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55
Q

What is the effect of noncompetitive inhibitors on Km & Vmax?

A

Km: does not change
Vmax: decreases (will take longer to reach Vmax)

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56
Q

What does Gibb’s free energy measure?

A

The amount of energy available to see if a reaction is energetically feasible

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57
Q

If Gibbs free energy is positive, what does this mean? (Triangle G)

A

Reaction is non-spontaneous (endorgonic) & unfavorable

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58
Q

If Gibbs free energy is neutral, what does this mean? (Triangle G)

A

The reaction is at equilibrium

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59
Q

If Gibbs free energy is negative, what does this mean? (Triangle G)

A

Reaction is spontaneous (exergonic) & favorable

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60
Q

Vitamins are converted into __________ while minerals are converted into ____________.

A

Vitamins -> Coenzymes
Minerals -> Cofactors

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61
Q

The term reduction means

A

Gaining a hydrogen

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62
Q

What is the most active form of Iron?

A

Fe3+ (Ferric)

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63
Q

What is the most absorbable form of iron?

A

Fe2+ (Ferrous)

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64
Q

1) What form of Iron is found in food?
2) What form is absorbed by intestines?
3) What form is used by the body?

A

1) Fe3+
2) Fe2+
3) Fe3+

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65
Q

1) What converts Fe3+ to Fe2+?
2) What converts it back to Fe3+ to be used in the body?

A

1) Vitamin c
2) Cu2+

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66
Q

A deficiency of ____________ or ___________ results in tetany. Why?

A

Mg or Ca; because they track together

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67
Q

What vitamins and minerals are antioxidants?

A

Vitamins A,C,E
Selenium
Glutathione
Lipoic Acid
CoQ10

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68
Q

What hormone increases serum calcium?

A

PTH

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69
Q

What hormone decreases serum calcium?

A

Calcitonin

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70
Q

In monosaccharides, the aldehyde group is always on __________ and the ketone is always ___________.

A

C=O on Carbon #1; C=O on Carbon #2

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71
Q

If there are 5 carbons on a monosaccharide it is known as ____________. 6 carbons?

A

5: Pentose
6: hexose

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72
Q

What is a Carbonyl group?

A

C=O (double carbon bond to Oxygen)

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73
Q

What monosaccharides are aldohexoses?

A
  • Glucose
  • Galactose
  • Mannose
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74
Q

What monosaccharides are aldopentoses?

A

Ribose

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75
Q

What monosaccharides are ketohexoses?

A

Fructose

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76
Q

What is the Monosaccharide formula?

A

Cn(H20)n
Where “n” is the number of carbons
Multiply the 2 by the number of carbons***

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77
Q

What is an isomer?

A

Different compounds with the same chemical formula

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78
Q

Examples of isomers

A

Glucose, Fructose & Galactose (C6H12O6)

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79
Q

What is an epimer?

A

Monosaccharide that differs around one specific carbon

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80
Q

What 2 substances are C-4 epimers?

A

Glucose & Galactose

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81
Q

What 2 substances are C2 epimers?

A

Glucose & Mannose

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82
Q

What is an Enantiomer? Example?

A

Mirror image of the same compound
L and D-Glucose

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83
Q

When are Anomers formed?

A

When sugars cyclize; and they are designated either alpha or beta

84
Q

Fischer projection vs. Haworth projection of monosaccharides:

A

Fischer: linear stick figure
Haworth: Cyclized form

85
Q

Sucrose is _____________ (__) + _____________ (__)

A

Glucose (alpha 1) + Fructose (beta 2)

86
Q

Lactose is _____________ (__) + _____________ (__)

A

Galactose (beta 1) + Glucose (beta 4)

87
Q

Maltose is _____________ (__) + _____________ (__)

A

Glucose (alpha 1) + Glucose (alpha 4)

88
Q

Isomaltose is _____________ (__) + _____________ (__)

A

Glucose (alpha 1) + Glucose (alpha 6)

89
Q

Cellobiose is _____________ (__) + _____________ (__)

A

Glucose (beta 1) + glucose (beta 4)

90
Q

What can break (beta 1, beta 4) in lactose?

91
Q

Amylopectin breaks into…

A

Maltose & isomaltose

92
Q

What can break (alpha 1, alpha 4) linkages to form maltose?

93
Q

Amylos ebreaks only into

94
Q

What is known as homopolymers of glucose?

A

Polysaccharides

95
Q

Polysaccharides in humans:

96
Q

Polysaccharides in plants:

A

1) Amylose
2) Amylopectin
3) Cellulose

97
Q

What is the branch point of glycogen?

A

Alpha 1,6 linkage

98
Q

What breaks amylose into maltose?

A

Alpha-amylase

99
Q

What are Glycosaminoglycans (GAGs)?

A

Large complex of negatively charged heteropolysaccharides which bind large amounts of water

100
Q

What is the major structural unit of Glycosaminoglycans (GAGs)?

A

Repeating disaccharides unit (protein sugar molecules)

101
Q

What are the most common GAGs?

A

Hyaluronic Acid in synovial fluid & Chondroitin Sulfate in cartilage, tendons and ligaments

102
Q

What type of bonds is a characteristic of fats?

A

Ester bonds

103
Q

Triacylglycerols have __________________ esterified to a ___________ ____________.

A

3 fatty acids; glycerol backbone

104
Q

A glycerol backbone consists of:

A

An acid + an alcohol

105
Q

An ester bond consists of a n

A

Alcohol + acid

106
Q

What are the most predominant form of fats/lipids in the body & diet?

A

Triacylglycerols

107
Q

Where does glycerol come from?

108
Q

What are fatty acids composed of?

A

Nonpolar hydrocarbon tails & polar carboxylic acid head

109
Q

What type of bond do unsaturated fatty acids have?

A

Double bonds

110
Q

What do double bonds do to melting and freezing points of fatty acids?

A

Melting point: decreases it
Freezing point: raises

111
Q

Naturally occurring double bonds exist in what configuration?

A

Cis configuration

112
Q

What 3 things does Hydrogenation do?

A

1) raises melting point / decreases freezing point
2) increases shelf life
3) makes trans fats

113
Q

Oxidation involves _____ of a Hydrogen

114
Q

Reduction involves _____ of a hydrogen

115
Q

To generate an unsaturated fat from a saturated fat _______ is required

116
Q

What are the essential fatty acids?

A

Linoleic acid (omega 6)
Linolenic acid (omega 3)
Arachidonic acid (omega 6)

117
Q

What is Linoleic acid (omega 6) found in?

A

Sunflower, safflower and corn oil

118
Q

What is Linolenic acid (Omega 3) found in?

119
Q

What is arachidonic acid (omega 6) found in?

A

Animal products (diary & red meat)

120
Q

What is the precursor to prostaglandins?

A

Arachodonic acid

121
Q

What is the most saturated oil?

A

Coconut oil

122
Q

4 Saturted fats:

A

1) Laurie acid
2) myristic acid
3) palmitic
4) stearic

123
Q

4 Unsaturated fats:

A

1) Oleic acid
2) Linoleic acid
3) Linolenic acid
4) arachidonic acid

124
Q

How many Carbons do the following have?
1) Lauric Acid
2) Myristic Acid
3) Palmitic Acid
4) Stearic Acid

A

1) 12
2) 14
3) 16
4) 18

125
Q

Oleic Acid has how many carbons and how many (C=C) bonds?

A

18 / (1 C=C)

126
Q

Linoleic Acid has how many carbons and how many (C=C) bonds?

A

18 / (2 C=C)

127
Q

Linolenic Acid has how many carbons and how many (C=C) bonds?

A

18 / (3 C=C)

128
Q

Arachodonic Acid has how many carbons and how many (C=C) bonds?

A

20 / (4 C=C)

129
Q

Phospholipids contain

A

2 fatty acids & a polar head group which is esterified to glycerol-3-phosphate

130
Q

What is the major component of membrane lipids?

A

Phospholipids

131
Q

What are the 2 classes of non glycerol lipids?

A

Sphingolipids & Steroids

132
Q

What is the major lipid component of myelin sheath?

A

Sphingomyelin

133
Q

A deficiency of sphingomyelinase results in

A

Niemann-Pick Disease

134
Q

What is the most abundant Sterol in humans?

A

Cholesterol

135
Q

Cholesterol is derived from…

A

acetyl CoA

136
Q

Path of Acetyl CoA to steroid hormones (6 steps)

A

Acety CoA -> HMG-CoA -> Mevalonate -> Squalene -> Cholesterol -> Steroid hormones

137
Q

What is the rate limiting enzyme of cholesterol synthesis?

A

HMG-CoA reductase

138
Q

What does HMG-CoA reductase do?

A

Converts HMG-CoA -> mevalonate

139
Q

What is the rate limiting enzyme in Steroid biosynthesis is…

140
Q

What does the enzyme desmolase do?

A

Converts cholesterol -> pregnenolone -> progesterone

141
Q

Where is cholesterol eliminated?

142
Q

What 2 things bind to increase elimination of cholesterol?

A

Fiber & Bile Salts

143
Q

What is the rate limiting enzyme of Ketone body synthesis?

A

HMG-CoA Synthase

144
Q

Lipoproteins are composed of

A

A monolayer of polar lipids and proteins which surround a hydrophobic core of cholesterol esters and/or triglycerides

145
Q

Where are chylomicrons produced and secreted from?

A

Intestinal mucosal cells in response to dietary intake of fats

146
Q

What carries triacylglycerides to peripheral tissues?

A

Chylomicrons
VLDL (from liver to peripheral tissues)

147
Q

Where are VLDL synthesized and secreted from?

148
Q

LDL is derived from…

A

VLDL
VLDL -> IDL -> LDL

149
Q

Function of LDL

A

Transport cholesterol from liver to peripheral tissues

150
Q

What contains the most cholesterol?
VLDL
Chylomicrons
LDL
HDL

151
Q

Where is HDL synthesized and secreted from?

152
Q

Function of HDL:

A

Transport cholesterol from peripheral tissues back to the liver

153
Q

High LDL levels ________ risk of Heart disease

154
Q

High plasma levels ______ risk of heart disease

155
Q

What enzyme is required for the uptake of triglycerides carried by VLDL and Chylomicrons?

A

Lipoprotein Lipase

156
Q

List the Lipoproteins from highest density to lowest:

A

HDL, LDL, IDL, VLDL, Chylomicrons

157
Q

List the Lipoproteins from Biggest to Smallest in size:

A

Chylomicrons, VLDL, IDL, LDL, HDL

158
Q

What are DNA and RNA composed of?

A

Phosphate, pentose sugar & nitrogenase base

159
Q

What pentose sugar is in DNA? RNA?

A

DNA: deoxyribose
RNA: ribose

160
Q

The formation of deoxyribose from ribose is what type of reaction?

A

Reduction because you gained a hydrogen

161
Q

The purine nitrogenous bases are…

A

Adenine & Guanine

162
Q

Purine Nitrogen is derived from what amino acids: (3)

A

Aspartate
Glycine
Glutamine

163
Q

What is the rate limiting enzyme of purine breakdown?

A

Xanthine oxidase

164
Q

What are the Pyrimidines of DNA and RNA?

A

DNA: Thyine
RNA: Uracil
BOTH: Cytosine

165
Q

Nucleosides = _____________ + _____________

A

Pentose sugar + nitrogenous base

166
Q

Nucleotides = _______________ + _____________ + _____________

A

Pentose sugar + nitrogenous base + phosphate

167
Q

What are the purines and pyrimidines of DNA?

A

Purines: adenine & guanine
Pyrimidines: cytosine & thymine

168
Q

What is DNA associated with?

169
Q

Histones are the chief component of ___________

A

Chromatin (they act as spools around which DNA winds)

170
Q

What is the base pairing pattern of DNA?

171
Q

What is the base pairing of RNA?

A

There is none, it’s single stranded

172
Q

What Pyrimidines replaces in RNA compared to DNA?

A

Uracil replaces Thymine

173
Q

What type of bonds are in DNA and RNA?

A

Phosphodiester bonds

174
Q

Phosphodiester bonds in DNA and RNA link between…

A

The 3 Carbon of one sugar and the 5 Carbon of another sugar

175
Q

Phosphodiester bonds are _________ bonds.

176
Q

Hydrogen bonds are only in _______. (DNA or RNA)

177
Q

DNA replication occurs in the _________ during the ________ of the cell cycle.

A

Nucleus; S Phase

178
Q

What direction does DNA replication follow?

A

From 5 carbon to the 3 carbon

179
Q

DNA replication is considered _______ and _________.

A

Anti-parallel & non-comparable

180
Q

What is the enzyme responsible for DNA replication?

A

DNA polymerase

181
Q

DNA transcription turns DNA into

182
Q

DNA Transcription occurs in the

183
Q

DNA Transcription follows what direction?

A

From the 5 Carbon to the 3 Carbon

184
Q

Every 3 bases in a strand of mRNA is called what?

185
Q

What does a single Codon do?

A

Encodes for a single amino acid

186
Q

What enzyme is responsible for DNA transcription?

A

RNA Polymerase

187
Q

What is the 1st amino acid that is coded during DNA transcription?

A

Methionine

188
Q

What are start codons?

A

AUG (MC)
GUG

189
Q

What are the stop codons?

A

UAA, UGA & UAG

190
Q

Translation occurs in the

A

Cytoplasm on the Rough ER

191
Q

Steps of Translation: (4)

A

1) ribosomes expose 2 codons
2) codon recognized by anticodon on tRNA molecule
3) tRNA is bound to a specific amino acid
4) peptidyl transferase links 2 amino acids to begin synthesis of polypeptide chain

192
Q

Steps of protein synthesis: (3)

A

1) Ribosomes read mRNA in 5 -> 3 carbon direction
2) synthesis proceeds from N to C terminus
3) always add amino acid @ C terminus during translation

193
Q

Reverse transcription brings ______ back to ______

194
Q

Examples of Catablic pathways: (3)

A

1) GLycolysis
2) lipolysis
3) glycogenolysis

195
Q

What is a catabolic pathway?

A

Breakdown of macromolecules into simple precursors to generate ATP to reduce power (NADH, FADH)

196
Q

What is an Anabolic pathway?

A

Synthesis of macromolecules from simple precursors (ATP generated from catabolic pathways are used to drive anabolic reaction)

197
Q

Examples of anabolic pathways: (4)

A

1) gluconeogenesis
2) lipogenesis
3) glycogenesis
4) Nucleic acid synthesis

198
Q

Definition of Phosphatase

A

Removes a phosphate

199
Q

Definition of Phosphorylase

A

Adds a phosphate

200
Q

Definition of Kinase

A

Moves a phosphate around

201
Q

Dehydrogenase is used in

A

Oxidation and reduction reactions

202
Q

Definition of Carboxylase

A

Add a carbon

203
Q

Definition of decarboxylase

A

Removes a carbon

204
Q

What amino acids are NOT glucogenic?

A

Leucine & Lysine

205
Q

What amino acids are neutral?

A

Serine, Threonine, Asparagine, Glutamine

206
Q

What amino acids donate Nitrogen for purines & Pyrimidines?

A

Glutamine, Aspartate & Asparagine

207
Q

What is the # of Carbons in Arachodonic Acid?

A

20 (count in answer choices to eliminate)

Part 1 Boards (12 decks)

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