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BSR - Biochem > Worksheets > Flashcards

Worksheets Flashcards

1
Q

List the 9 Amino acids with non polar side chains.

A

Glycine, alanine, valine, leucine, isoleucine, phenylalanine, tryptophan, methionine, proline

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2
Q

Which of the non polar amino acids has a secondary amino group and may be referred to as an imino acid?

A

Proline

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3
Q

Are non polar amino acids hydrophobic or hydrophilic?

A

hydrophobic

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4
Q

Which non polar amino acid can contribute to a disulfide bond?

A

Methionine

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5
Q

Which non polar amino acid is used to form serotonin?

A

Tryptophan

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6
Q

List the 6 amino acids with uncharged polar side chains.

A

Asparagine, cysteine, glutamine, serine, threonine, tyrosine

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7
Q

Which amino acid with an uncharged polar side chain is used to form dopamine?

A

Tyrosine

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8
Q

List the 2 amino acids with acidic side chains.

A

Aspartic & glutamic acid

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9
Q

List the 3 amino acids with basic side chains.

A

Histidine, lysine, arginine

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10
Q

Are all amino acids found in proteins in people of the D or of the L configuration?

A

L

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11
Q

In sickle cell anemia, the amino acid _______ is substituted for glutamate at the sixth position in the beta subunit of hemoglobin.

A

valine

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12
Q

In hemoglobin C disease, the amino acid _______ is substituted for glutamate at he sixth position in the beta subunit of hemoglobin.

A

lysine

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13
Q

The sequence of amino acids in a protein is referred to as the ______ structure of a protein.

A

primary

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14
Q

Alpha helix, beta sheets, and beta bends are examples of the _______ structure of a protein.

A

secondary

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15
Q

The three dimensional shape of a folded protein is referred to as the _______ structure of a protein.

A

Tertiary

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16
Q

Arrangement of multiple poly-peptide subunits in the protein are referred to as the _______ structure of a protein.

A

Quaternary

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17
Q

Primary, secondary, tertiary, and quaternary structure all contribute to the ______ _______ of the protein.

A

Native confirmation

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18
Q

Specialized groups of proteins named ______ are required for proper folding of some nascent peptides.

A

Chaperones

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19
Q

Unfolding and disorganization of the protein’s secondary and tertiary structure is referred to as ________ of the protein.

A

denaturation

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20
Q

Misfolding of proteins and abnormal tau proteins, may result in amyloids and neurofibrillary tangles, which are characteristics of _______ disease.

A

Alzheimer’s

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21
Q

As altered version of a prion protein can cause a group of diseases known as transmissible spongiform encephalopathies (TSEs). An example in humans is _____________ disease.

A

Creutzfeldt - Jakob

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22
Q

In proteins, amino acids are joined covalently by ______ bonds, which are amide linkages between the alpha carboxyl group of one amino acid and the alpha carboxyl group of one amino acid and the alpha amino group of another.

A

peptide

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23
Q

Hemoglobin ____ is the major hemoglobin in adults. It is comprised of two _____ and two _____ chains. Hemoglobin can carry _____ oxygen molecule(s).

A

A ; alpha ; beta ; 4

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24
Q

Myoglobin is a hemeprotein present in _____ and ______ muscle. Myoglobin can reversibly bind ____ oxygen molecule(s).

A

heart; skeletal; 1

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25
Q

The myoglobin oxygen dissociation curve is described as ______. The hemoglobin oxygen dissociation curve is described as ______.

A

hyperbolic ; sigmoidal

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26
Q

Cooperative binding of oxygen by the four subunits of hemoglobin means the binding of an oxygen molecule at one heme group ______ the affinity for oxygen of the remaining heme groups in the same hemoglobin molecule.

A

increases

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27
Q

With the ____ effect, release of oxygen from hemoglobin is enhanced when the pH is ______ and the pCO2 is _______. This is also described as a shift to the _____ of the oxygen dissociation curve.

A

Bohr ; lowered ; increased; right

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28
Q

Lungs have a _____ pH, tissues have a ____ pH.

A

higher ; lower

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29
Q

Carbon monoxide shifts the oxygen dissociation curve to the ____, thus decreasing the ability of hemoglobin to release oxygen to tissues.

A

left

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30
Q

Hemoglobin ___ is themajor hemoglobin found in the fetus and newborn. Fetal hemoglobin has a _____ affinity for oxygen compared to hemoglobin A.

A

F ; higher

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31
Q

Increased amounts of hemoglobin _____ are found in RBC’s of patients with diabetes mellitus. This type of hemoglobin is described as ______ hemoglobin.

A

A1C ; glycosylated

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32
Q

______ is a hereditary hemolytic disease in which an imbalance occurs in the synthesis of glob in chains of hemoglobin.

A

Thalassemias

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33
Q

_______ is the most abundant protein in the body and includes three alpha chains which form a triple helix.

A

Collagen

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34
Q

_______ is a group of connective tissue disorders, which result in fragile, stretchy skin and loose joints.

A

Ehlers - Danlos Syndrome (EDS)

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35
Q

__________ is a group of connective tissue disorders, which result in bones that easily bend and fracture.

A

Osteogenesis imperfecta (OI)

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36
Q

Alpha 1 -Antitrypsin prevents elastin degradation in the _____ walls. A deficiency of alpha 1-antitrypsin can cause a lung disease called _____.

A

alveolar ; emphysema

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37
Q

Mutations in the fibrillin -1 protein are responsible for ____ syndrome.

A

Marfans

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38
Q

_______ are protein catalysts that increase the rate of reactions without being changed in the overall process.

A

Enzymes

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39
Q

Statin dugs are examples of ______ inhibitors. They compete effectively to inhibit the enzyme _______ , thereby inhibiting de novo cholesterol synthesis.

A

competitive ; HMG CoA reductase

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40
Q

The presence of elevated levels of the enzyme alanine aminotransferase (ALT) in plasma signals damage to _____ tissue.

A

hepatic

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41
Q

Elevation of the fraction of the isoenzymes of creatine kinase (CK) referred to as CK2 or MB indicates damage to the ______, whereas elevation of CK3 or MM only signals damage to _______.

A

myocardium ; skeletal

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42
Q

Troponins are regulatory proteins that are highly sensitive and specific for damage to ______ tissue.

A

cardiac

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43
Q

Enthalpy and entropy can be used to determine a third quantity called ______ which predicts the direction in which a reaction will spontaneously proceed.

A

free energy

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44
Q

If free energy (delta G) is negative, there is a net _____ of energy, and the reaction _____ go spontaneously.

A

loss ; will

45
Q

A reaction with a positive standard free energy can proceed if the ratio of products to reactants in sufficiently _____.

A

low

46
Q

The electron transport chain is present in the inner ______ membrane and is th final common pathway by which ______ derived from different fuels of the body flow to oxygen. Complex V catalyzes _____ synthesis

A

mitochondrial ; electrons ; ATP

47
Q

Coenzyme Q, also called ______ is a mobile carrier that links the ______ to the _______ in the e- transport chain.

A

ubiquinone ; flavo proteins ; cytochromes

48
Q

________ is the substrate for Complex I. ________ is the substrate for complex II.

A

NADH dehydrogenase ; succinate dehydrogenase

49
Q

Incomplete reduction of oxygen to water produces ____ ___ ____ (ROS), which can damage ____ and _____ and cause lipid ____.

A

reactive oxygen species ; DNA ; Proteins ; peroxidation

50
Q

Redox pairs: ______ (loss of electrons) of one compound is always accompanied by ______ (gain of e-) of a second substance.

A

oxidation ; reduction

51
Q

The empiric formula for the simpler carbs is _____

A

(CH2O)N

52
Q

Simple sugars are called _____. Three carbon simple sugars are called _____ and an example is ______.

A

monosaccharides ; trioses ; glyceraldehyde

53
Q

Five carbon simple sugars are called _____ and an example is ______.

A

pentoses ; ribose

54
Q

Six carbon simple sugars are called ____, and an example is _____.

A

hexoses ; glucose

55
Q

Monosaccharides can be linked by ______ bonds.

A

glycosidic

56
Q

Carb digestion begins in the mouth with salivary _____. it halts in the stomach due to low pH, but continues again in the small intestine with pancreatic _____.

A

amylase ; amylase

57
Q

Three quarters of the world’s adults are deficient in the enzyme _____ and therefore are unable to digest____.

A

lactase ; lactose

58
Q

The first stage of catabolism is _______ of complex molecules such as carbs, proteins, and fats.

A

hydrolysis

59
Q

The second stage in conversion of building blocks to simple intermediates, primarily _____.

A

Acetyl CoA

60
Q

The third stage is _____ of acetyl coA in the ______ cycle.

A

oxidation ; tricarboxylic acid

61
Q

______ is the end product of glycolysis in cells with mitochondria and an adequate supply of oxygen. Conversion of glucose to lactate is called _______ glycolysis because it can occur without the participation of oxygen in cells that pact mitochondria.

A

pyruvate ; anaerobic

62
Q

Of the 14 glucose transporter isoforms, GLUT- ___ is abundant in erythrocytes and blood brain barrier, GLUT- ___ in neurons, and GLUT-___ in _____ tissue and _______.

A

1 ; 3 ; 4; adipose ; skeletal ms.

63
Q

The first five steps of glycolysis are considered an energy _____ phase. The last five steps of glycolysis is considered an energy _____ phase. The ten steps taken together give a net gain of ___ molecules of ATP per molecule of glucose.

A

investment ; generation ; 2

64
Q

In most tissues, phosphorylation of glucose is catalyzed by ______. I the liver parenchymal cells and beta cells of the pancreas, this function is carried out by a related enzyme called ______.

A

hexokinase ; glucokinase

65
Q

This irreversible phosphorylation of fructose 6-phosphate is catalyzed by _____, and is the most important control point and the rate-limiting and committed step of glycolysis. Conversion of phosphoenolpyruvate (PEP) to pyruvate is catalyzed by ______.

A

fructokinase-1 ; pyruvate kinase

66
Q

_________ deficiency accounts for 95% of all inherited defects in glycolytic enzymes. This deficiency results in mild to severe ____ _____ amenia.

A

pyruvate kinase ; chronic hemolytic

67
Q

The TCA cycle is also called the ____ cycle or the _____ cycle. The TCA cycle is an erobic pathway, because oxygen is required as the final e- _____.

A

citric acid ; krebs ; acceptor

68
Q

_____ NADH, __ FADH2, and ___ GTP are produced by one round of the TCA cycle. There are a total of ___ ATP produced from the complete mitochondrial oxidation of one molecule of acetyl CoA.

A

3; 1; 1; 12

69
Q

The hormone _____ from the alpha cells of the pancreatic islets stimulates gluconeogenesis

A

glucagon

70
Q

Synthesis of glycogen is called ____. Degradation of glycogen is called ______. These processes take place in the _____ of the cell.

A

glycogenesis; glycogenolysis ; cytosol

71
Q

90% of the average daily intake of lipids by US adults in normally ______, formerly called triglyceride.

A

triacylglycerol (TAG)

72
Q

The digestion of lipids begins in the ____ , catalyzed by acid-stable enzymes called ______.

A

mouth ; lingual lipase

73
Q

Digestion of lipids continues in the _____ . Enterocytes reassemble lipids with apoprotein B-48 to form _____, which are secreted into the _____ system where they are transported to the ____.

A

SI ; chylomicrons ; lymph ; blood

74
Q

Patients with _____ have difficulties with digestion of lipids because their thickened pancreatic secretions are less able to reach the SI. Excess lipid in feces is termed _____.

A

cystic fibrosis; steatorrhea

75
Q

Triacylglycerol (TAG) is degraded to ______ and _____ by ______.

A

free fatty acids ; glycerol ; lipoprotein lipase

76
Q

Unsaturated fatty acids contain one or more _______.

A

double bonds

77
Q

Arachidonic acid, 20:4(5,8,11,14) contains _____ carbon atoms and has ____ double bonds between carbons 5-6, 8-9, 11-12, 14-15.

A

20 ; 4

78
Q

The two fatty acids that are dietary essentials in humans are ____ ____ and ___ ___ ___.

A

linoleic acid ; alpha-linolenic acid

79
Q

______ is the precursor of all classes of steroid hormones.

A

cholesterol

80
Q

______ is the major disposal form of amino groups. It is produced by the ____ and is transported to the ____ for excretion in the ____.

A

urea ; liver ; kidney ; urine

81
Q

DNA and RNA purines include ____ & _____.

A

adenine and guanine

82
Q

DNA pyrimidines include _____ & _____.

A

cytosine and thymine

83
Q

RNA pyrimidines include _____ & _____.

A

cytosine and uracil

84
Q

Nucleotides are composed of a _____ base, a _____ monosaccharide, and one, two or three _____ groups.

A

nitrogenous ; pentase ; phosphate

85
Q

_____ is the end product of purine degradation. A diet rich in meat and shellfish is associated with increased risk of a condition referred to as _____.

A

uric acid ; gout

86
Q

How is the dissociation constant Ka calculated?

A

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

87
Q

The larger the Ka, the ____ the acid.

A

stronger

88
Q

Write out the Henderson -Hasselbalch equation.

A

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

89
Q

What does a buffer do?

A

Resists change in pH following the addition of an acid or a base.

90
Q

Maximum buffering occurs when the pH is equal to ____

A

pka

91
Q

A zwitteron is the _____ form of an amino acid and has an overall (net) charge or ____

A

isoelectric ; zero

92
Q

Amphoteric electrolytes can act as an ____ or a ____

A

acid ; base

93
Q

The peptide bond has a partial _______ character.

A

double bond

94
Q

Peptide bonds are almost always ____ bonds, due to the steric interference of R groups when in the cis position.

A

trans

95
Q

Enzymes that hydrolyze peptide bonds are called _____.

A

peptidases

96
Q

The ____ form of hemoglobin is called the “T” or taut form.

A

deoxy

97
Q

The “R” form or relaxed form has a ____ oxygen affinity.

A

high

98
Q

______ effectors interact at one site of hemoglobin and affect binding of oxygen to another site.

A

allosteric

99
Q

The affinity of hemoglobin for the last oxygen bound is ____ times greater than its affinity for the first oxygen bound.

A

300

100
Q

2,3 - BPG _____ oxygen affinity of hemoglobin by binding to deoxyhemoglobin but not oxyhemoglobin, thereby stabilizing the “T” conformation.

A

decreases

101
Q

Hemoglobin deficient in 2,3 - BPG acts as an ____ trap.

A

oxygen

102
Q

Storing blood ______ 2,3 BPG.

A

decrease

103
Q

Binding of CO2 stabilizes the “T” or taut form of hgb, resulting in a ____ of its affinity for oxygen.

A

decrease

104
Q

Carbon monoxide causes hgb to shift to the ___ conformation, causing the remaining sites to bind oxygen with high affinity.

A

R

105
Q

Affinity of hemoglobin for CO is ____ times greater than for oxygen.

A

220

106
Q

Hemoglobin F has two ___ chains and two ____ chains.

A

alpha ; gamma

107
Q

Non enzymatic addition of sugar to a protein is called _____.

A

glycation

108
Q

At low oxygen tension, deoxyhemoglobin S ______ inside the RBC, forming a network of insoluble fibrous polymers that stiffen and distort the cell.

A

prolymerizes

109
Q

Malaria is caused by ________ _____

A

Plasmodium falciparum

BSR - Biochem (1 decks)

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