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Exam 1 Flashcards

Chapters 1, 2,27,28,29,5,6,7,8, & 15 (149 cards)

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1
Q

What are the non-polar amino acids?

Chapter 1: Amino Acids

A

Alanine
Glycine
Isoleucine
Leucine
Methionine
Proline
Valine

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2
Q

What amino acids have carboxyl groups?

Chapter 1: Amino Acids

A

Aspartic Acid
Glumatic Acid

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3
Q

What amino acids contain amine groups?

Chapter 1: Amino Acids

A

Arginine
Histidine
Lysine

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4
Q

What amino acids containe aromatic compounds?

Chapter 1: Amino Acids

A

Phenylalanine
Tryptophan
Tyrosine

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5
Q

What amino acids contain hydroxyl groups?

Chapter 1: Amino Acids

A

Serine
Threonine
Tyrosine

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6
Q

What are the properties of the primary protein structure?

Chapter 2: Protein Structure

A
  • linear sequence of amino acids
  • joined by peptide bonds
  • translated from mRNA
  • synthesis begins at the amino end and terminates at the carboxyl end
  • ultimately determines all properties of a protein
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7
Q

What are the properties of secondary structure?

Chapter 2: Protein Structure

A
  • hydrogen bonds stabalize structure
  • alpha helix and beta pleated sheets
  • different structures = different functions
  • Examples: collagen, keratin, fibroin
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8
Q

What are the properties of tertiary structure?

Chapter 2: Protein Structure

A
  • folding and turns
  • folding of globular proteins
  • unfolding of globular proteins
  • alpha and beta pleated sheets stay connected
  • hydrophobic bonds stabalize the structure
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9
Q

What are the properties of quanternary structure?

Chapter 2: Protein Structure

A
  • two or more polypetide chains
  • primarily held together by noncovalent interactions
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10
Q

What are the ways proteins are denatured and misfolded?

Chapter 2: Protein Structure

A
  • Mercaptoethanol/dithiotheitol: breaks disulfide bonds
  • Detergent: disrupts hydrophobic interactions
  • Heat: break hydrogen bonds
  • pH: can change charge or alter ionic interactions
  • chelators: bind metal ions
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11
Q

What are the paired amyloids to the following diseases?
1. Alzheimer’s Disease
2. Parkinson’s Disease
3. Huntingtin’s Disease
4. Rheumatiod Arthritis
5. Fatal familial insomnia

Chapter 2: Protein Structure

A
  1. Alzheimer’s Disease - Amyloid B
  2. Parkinson’s Disease- alpha synuclein
  3. Huntingtin’s Disease - Huntingtin
  4. Rheumatoid Arthritis - Serum Amyloid A
  5. Fatal Familial Insomnia - PrP sc
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12
Q

Chaperonins

Chapter 2: Protein Structure

A

Proper folding environment for hydrophobic sequences

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13
Q

Proteasomes

Chapter 2: Protein Structure

A

Degradation to oligopeptides of about 8 amino acids each

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14
Q

What is the role of Ubiquitin?

Chapter 2: Protein Structure

A

Flag for protein destruction by proteasome

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15
Q

What is the difference between nonessential and essential amino acids?

Chapter 27: Nutrition

A

Nonessential amino acids can be synthesized by the body from metabolic intermediates or from essential amino acids.
Essential amino acids cannot be synthesized by humans and must be obtained from the diet.

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16
Q

Monosaccharides

Chapter 27: Nutrition

A

glucose and fructose are principal monosacchatides found in food

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17
Q

Disaccharides

Chapter 27: Nutrition

A

Contain two monosaccharide untis( i.e. lactose, sucrose, maltose, etc.)

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18
Q

Polysaccharides

Chapter 27: Nutrition

A

Contain more than ten monosaccharide units , such as starch and glycogen

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19
Q

What is the recommended carbohydrate intake?

Chapter 27: Nutrition

A

130g/day
45-65% of total calories

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20
Q

What are the types of lipids?

Chapter 27: Nutrition

A

Saturated fatty acids (no double bonds)
Unsaturated fatty acids (double bonds)
Essential fatty acids
Omega- 3 (polyunsaturated fatty acids)
Omega -6
Triacylglycerols (main stage form of fatty acids)
Phospholipids
Steroids

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21
Q

What is the recommended intake of Lipids?

Chapter 27: Nutrition

A

20-35% of calories

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22
Q

What are the water soluble vitamins?

Chapter 28: Vitamins

A

Vitamin C
B-complex Vitamins

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23
Q

What are the fat-soluble vitamins?

Chapter 28: Vitamins

A
  • Vitamin D
  • Vitamin A
  • Vitamin E
  • Vitamin K
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24
Q

Vitamin A (Retional)

Chapter 28: Vitamins

A

Roles:
* Vision (precursor of retinal)
* Growth and reproduction (spermatogenesis , prevents fetal resorption)
* Differentiation and maintence of epithelial cells
* Gene expression
Deficiency
* Night blindness
* Xerophthalmia
* Decreased growth rate
* Weaked immune system
Toxicity
* Orange skin, fatigue, headaches
* Blurred vision, hair loss, joint pain
* liver/brain damage
* birth defects

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25
Vitamin D (Cholecalciferol) ## Footnote Chapter 28: Vitamins
Roles: * Maintains plasma calcium via intestinal absorption, kidney conservation, bone resorption * Bone formation * Immune system support Deficiency * Rickets(children) * Osteomalacia (adults) * Hypocalcemia Toxicity * Loss of appetite, nausea, thirst, stupor * Hypercalcemia, calcium deposition in organs
26
Vitamin E (Tocopherols) ## Footnote Chapter 28: Vitamins
Roles * Antioxidant (protects red bloos cells and muscle from oxidative damage) Deficiency * Rare, infertility (sperm inhibition) * Muscle/nerve lesions Toxicity * Rare; may act as blood thinner
27
Vitamin K (Phylloquinones) ## Footnote Chapter 28: Vitamins
Roles * Blood clotting (gamma-carboxylation of clotting proteins) * bone health Deficiency * hypoprothrombinemia * bleeding (hemorrhagic disease of newborns) Toxicity * from menadione: hemolysis, hyperbilirubinemia, kernicterus, brain damage
28
Thiamine ( Vitamin B1) ## Footnote Chapter 28: Vitamins
Roles * Carbohydrate metabolism * coenzyme in aldehyde transfer reactions Deficiency * Beri-beri (weight loss, heart issues, nuerological dsyfunction) * Fatigue, nausea, depression, nerve damage
29
Riboflavin(Vitamin B2) ## Footnote Chapter 28: Vitamins
Roles * Metabolism, red blood cell function * Coenzyme( FAD, FMN) Deficiency * Cheilosis, angular stomatitis * Dermatitis, dry/scaly skin
30
Niacin (Vitamin B3) ## Footnote Chapter 28: Vitamins
Roles: * Energy production, skin, nerves, digestion * Coenzyme (NAD+, NADP+) Deficiency * Pellagra ( 3Ds: dermatits, diarrhea, dementia --> death) Toxicity/ Use * used for hyperlipidemia
31
Pantothenic Acid (Vitamin B5) ## Footnote Chapter 28: Vitamins
Roles * Amino acid and glycogen metabolism * Steroid hormone regulation * Coenzyme(Pyridoxal phosphate) Deficiency * Nervous system disorders * Microcytic anemia * Homocysteinemia Toxicity * Neurological disorders (from excess)
32
Biotin (Vitamin B7) ## Footnote Chapter 28: Vitamins
Roles * Hormone formation , metabolism * Component of carboxylase enzymes Deficiency * Rare; can result from raw egg white consumption ( avidin) * Genetic defects in biotin-carboxylase linkage * Skin and hair health issues
33
Folic Acid (Vitamin B9) ## Footnote Chapter 28: Vitamins
Roles * One-carbon metabolism * DNA synthesis (amino acids, pruines, TMP) * Blood cell formation and cell division Deficiency * Megaloblastic anemia * Neural tube defects (pregnancy risk) * Elevated homocysteine Prevalance * Most common vitamin deficiency in the US
34
Cobalamin ( Vitamin B12) ## Footnote Chapter 28: Vitamins
Roles * Coenzyme for : homocysteine --> methionine and Methylmalonyl CoA isomerization * Nervous system and DNA synthesis Deficiency * Megaloblastic anemia * Pernicious anemia (intrinsic factor deficiency ) * Neurological symtpoms (sometimes without anemia) Side bar: synthesized only by microorganisms (not in plants)
35
Vitamin C (Ascorbic Acid) ## Footnote Chapter 28: Vitamins
Roles * Antioxidant * Coenzyme in collagen synthesis * Supports bone, vessels, immunity, iron absorption Deficiency * Scurvy ( swollen/bleeding gums, hemorrhages) * Microcytic hypochromic anemia * Poor iron absorption
36
Calcium (Ca 2+) ## Footnote Chapter 29: Minerals
**Functions** * Most abundant mineral (bones and teeth) * Muscle contraction * Blood coagulation ( Factor IV) * Cellular Signaling **Deficiency (Hypocalcemia) *** Bone demineralization * Osteporosis **Toxicity ( Hypercalcemia) ** * Constipation Kideny stones Cardia arrest Calcium deposition in organs*
37
Iron (Fe) ## Footnote Chapter 29: Minerals
**Functions ** * Part of heme,myoglobin, cytochromes * oxygen transport in blood **Deficiency** * Most widespread mineral deficiency worldwide * Microcytic hypochromic anemia * Symptoms: apathy, low oxygen delivery to cells
38
Iodine ## Footnote Chapter 29: Minerals
**Functions** * Required for thyroid hormone synthesis (T3,T4) **Deficiency ** * Cretinism (children) * Goiter
39
Sodium (Na+) ## Footnote Chapter 29: Minerals
Functions * Water balance and osmotic equilibrium * Acid-base balance * Electrical gradients across membranes * Glucose and amino acid absorption Toxicity (excess intake) * Hypertension * Fluid retention
40
Potassium (K+) ## Footnote Chapter 29: Minerals
**Functions** * Water balance and osmotic equilibrium * Acid-base balance * Electrical gradients (nerve and muscle function) **Deficiency (Hypokalemia**) * Cardiac arrhythmias * skeletal muscle weakeness **Excess (Hyperkalemia)** * Cardiac arrhythmias * skeletal muscle weakeness
41
Magnesium (Mg 2+) ## Footnote Chapter 29: Minerals
Functions * Forms Mg-ATP complex (energy metabolism) * Needed for DNA/RNA polymerases (phosphodiester bonds) * Muscle contraction Deficiency * Muscle weakeness
42
What are symptoms of Marasmus? ## Footnote Chapter 29: Minerals
* Extreme emaciation and wasting * Arrested growth * Serve muscle wasting * loss of subcutaneous fat * Weakness, anemia * No edema * Body weight < 60% of expected
43
What are the symptoms of Kwashiorkor? ## Footnote Chapter 29: Minerals
* Edema( fluid retention) - key distringuishing sign * apathy, listlessness, poor appetite * fatty liver infiltration * low hemoglobin and plasma albumin * mild/absent muscle wasting * Body weight = 60-80% of expected
44
What is the general structure of an amino acid?
Alpha carbon + carboxyl group + hydrogen + R group
45
What is the chirality of most amino acids in biology?
Most are L-isomers
46
Name a category of amino acids based on R group properties: Nonpolar/aliphatic.
Gly, Ala, Val, Leu, Ile, Met, Pro
47
Name a category of amino acids based on R group properties: Aromatic.
Phe, Try, Trp
48
Name a category of amino acids based on R group properties: Polar uncharged.
Ser, Thr, Cys, Asn, Gln
49
Name a category of amino acids based on R group properties: Acidic.
Asp, Glu
50
Name a category of amino acids based on R group properties: Basic.
Lys, Arg, His
51
What is the primary structure of a protein?
Linear amino acid sequence
52
What is the secondary structure of a protein?
Local folding into alpha helices and beta sheets
53
What is the tertiary structure of a protein?
3D fold of a single polypeptide
54
What is the quaternary structure of a protein?
Multiple polypeptides assembled
55
What characterizes an alpha helix?
Right-handed helix, ~3.6 residues/turn, H-bonds between residues i and i + 4
56
What characterizes a beta sheet?
Extended, pleated strands, can be parallel or antiparallel, stabilized by inter-strand hydrogen bonds
57
What are the main forces that stabilize protein structure?
Hydrogen bonds, disulfide bonds, hydrophobic interactions, ionic interactions
58
What are the factors that can lead to denaturation of proteins?
Heat, pH changes, Detergents, Reducing agents, Metal ion chelators
59
What is the basic concept of protein folding?
Guided by energetics and sometimes chaperones; misfolding can be harmful.
60
How does protein structure relate to function?
Enzymes: active site shape enables catalysis Structural proteins: stable secondary/tertiary structures provide strength and support
61
What are some examples of post-translational modifications?
Phosphorylation, Glycosylation, Hydroxylation, Ubiquitin
62
What is the significance of post-translational modifications?
They regulate activity, stability, localization, and interactions of proteins.
63
What is the relationship between protein misfolding and diseases?
Misfolding leads to aggregates (amyloids/prions) that are often insoluble; related to diseases like Alzheimer's and Parkinson's.
64
What are examples of diseases related to protein misfolding?
1. Alzheimer’s (Amyloid Beta) 2. Parkinson’s (alpha-synuclein) 3. Huntington’s (huntingtin) 4. Rheumatoid arthritis (serum amyloid A) 5. Fatal familial insomnia (PrP SC)
65
What role do chaperones play in protein folding?
Chaperones assist in the proper folding of proteins, preventing misfolding and aggregation.
66
What role do chaperones play in protein folding?
They help correct misfolding of proteins.
67
What is the function of the proteasome and ubiquitin system?
They degrade damaged or misfolded proteins.
68
What are macronutrients?
Nutrients required by the body in large amounts providing energy; includes proteins, fats, and carbohydrates.
69
What are micronutrients?
Vitamins and minerals necessary for normal body function needed in smaller quantities.
70
What is the RDA for adults for proteins?
The Recommended Dietary Allowance (RDA) for adults for proteins is 46 grams per day for women and 56 grams per day for men.
71
What is the RDA for adults for proteins?
0.8g/kg with an acceptable macronutrient distribution range of 10-35% total daily calories.
72
What is the primary function of carbohydrates?
They are the primary source of energy for the body; glucose fuels the brain and red blood cells.
73
What are the types of carbohydrates?
Monosaccharides (glucose, fructose), disaccharides (sucrose, lactose), polysaccharides (starch, glycogen).
74
What is the RDA for carbohydrates in adults?
130 g/day, with an acceptable macronutrient distribution range of 45-65% of total calories.
75
What are the types of fats (lipids)?
Saturated, monounsaturated, polyunsaturated fatty acids (omega-3 and omega-6), phospholipids, and cholesterol.
76
What are the sources of high-quality proteins?
Animal sources like meat, milk, and fish that contain all essential amino acids.
77
What are the functions of proteins?
Building blocks for tissue, enzymes, structural components, transport molecules, hormones, immune defense.
78
What are the functions of fats in the body?
Concentrated energy source, Structural basis of cell membranes, Precursors for steroid hormones and prostaglandins, Aid in absorption of fat-soluble vitamins
79
What are the sources of saturated fats?
Dairy products, Meat products
80
What are the sources of unsaturated fats?
Vegetable oils, Fish
81
What is the RDA for fats?
20-35% of total calories
82
What is Protein-Energy Malnutrition (PEM)?
A widespread issue caused by inadequate intake of protein and/or energy.
83
What is Marasmus?
Severe deficiency of both calories and protein, characterized by extreme muscle wasting, loss of fat, and weakness, but no edema.
84
What is Kwashiorkor?
Occurs when protein deprivation is greater than calorie reduction, with symptoms like growth issues, edema, skin lesions, and fatty liver.
85
What can essential fatty acid deficiency lead to?
Scaly dermatitis (ichthyosis), hair loss, and poor wound healing.
86
What are the symptoms of Scurvy?
Bleeding gums, loose teeth, and poor wound healing due to defective collagen synthesis.
87
What are the effects of Vitamin D deficiency in children and adults?
Rickets in children and osteomalacia in adults, leading to poor bone mineralization and skeletal deformities.
88
What does Beriberi result from?
Thiamine (Vitamin B1) deficiency, causing peripheral nerve damage, heart failure, and CNS lesions.
89
What are the symptoms of Pellagra?
Characterized by the 3 D’s: dermatitis, diarrhea, and dementia due to Niacin (Vitamin B3) deficiency.
90
What causes Megaloblastic Anemia?
Folate or Vitamin B12 deficiency, leading to impaired DNA synthesis and large, immature red blood cells.
91
What neurological issue can Vitamin B12 deficiency cause?
Irreversible neurological damage.
92
What is one of the earliest signs of Vitamin A deficiency?
Impaired ability to see in dim light (Night blindness).
93
What does Vitamin K deficiency cause?
Impaired blood clotting (Hemorrhagic Disease) ## Footnote Example: Vitamin K deficiency can lead to excessive bleeding.
94
How does the body obtain energy from food?
By breaking down macronutrients into monomers through digestion, which are then absorbed and metabolized to produce ATP. ## Footnote Example: Carbohydrates are broken down into glucose.
95
What is the Resting Metabolic Rate (RMR)?
Energy required for basic body functions at rest. ## Footnote Example: RMR accounts for the calories burned while sleeping.
96
What does the Thermic Effect of Food refer to?
The energy expenditure above the resting metabolic rate due to the cost of processing food for use and storage.
97
Which component of energy expenditure is the most variable?
Physical Activity
98
How many kcal/g do fats provide?
9 kcal/g
99
What is the protein-sparing effect of carbohydrates?
Consuming adequate carbohydrates prevents the body from breaking down protein to produce glucose via gluconeogenesis.
100
What are the functions of Vitamin A?
Functions include vision, immune function, and skin health.
101
What are the sources of Vitamin A?
Animal products and carrots (as β-carotene).
102
What is the RDA for Vitamin A?
700-900 retinol activity equivalents.
103
What deficiency causes night blindness?
Vitamin A deficiency.
104
What can hypervitaminosis A cause?
Birth defects and liver damage.
105
What is the function of Vitamin D?
Regulates calcium and phosphate levels and is essential for bone health.
106
What vitamin is synthesized in the skin upon sunlight exposure?
Vitamin D
107
What deficiency causes rickets in children?
Vitamin D deficiency.
108
What deficiency causes rickets in children?
Vitamin D deficiency
109
What vitamin is a major lipid-soluble antioxidant?
Vitamin E (Tocopherol) ## Footnote Example: Vitamin E protects cell membranes from oxidative damage.
110
What deficiency can cause hemolytic anemia in premature infants?
Vitamin E deficiency
111
What vitamin is required for blood clotting factors?
Vitamin K
112
What deficiency can cause bleeding, especially in newborns?
Vitamin K deficiency
113
What is the coenzyme for pyruvate dehydrogenase?
Thiamine (B1)
114
What deficiency causes beriberi?
Thiamine (B1) deficiency
115
Which vitamin forms FAD and FMN?
Riboflavin (B2)
116
What vitamin forms NAD and NADP?
Niacin (B3)
117
What deficiency causes pellagra?
Niacin (B3) deficiency
118
What is the coenzyme for aminotransferases in amino acid metabolism?
Pyridoxine (B6)
119
What vitamin is a coenzyme for carboxylase enzymes?
Biotin (B7)
120
What vitamin is a coenzyme for carboxylase enzymes?
Biotin
121
What is the coenzyme for one-carbon transfers essential for nucleotide synthesis?
Folate
122
What deficiency causes megaloblastic anemia and neural tube defects?
Folate deficiency
123
What vitamin is a coenzyme for methionine synthase?
Cobalamin (B12)
124
What deficiency causes pernicious anemia?
Cobalamin (B12) deficiency
125
What vitamin acts as an antioxidant and is critical for collagen synthesis?
Vitamin C (Ascorbic Acid)
126
What deficiency causes scurvy?
Vitamin C deficiency
127
What is the most abundant mineral essential for bone structure?
Calcium
128
What is a key component of heme in hemoglobin?
Iron
129
What deficiency is the most common nutritional deficiency worldwide?
Iron deficiency
130
What does iron deficiency cause?
Microcytic anemia
131
What is the role of iodine in the body?
Required for the synthesis of thyroid hormones, which regulate metabolic rate.
132
What is iodine required for?
Iodine is required for the synthesis of thyroid hormones, which regulate metabolic rate.
133
What can iodine deficiency lead to?
Goiter and hypothyroidism.
134
What are vitamins?
Vitamins are organic compounds required in small amounts, often functioning as coenzymes in metabolic reactions.
135
What are fat-soluble vitamins?
Fat-soluble vitamins are vitamins A, D, E, K; absorbed with dietary fat and stored in the liver and adipose tissue.
136
What happens if fat-soluble vitamins are consumed in excess?
Excess consumption can lead to toxicity due to their storage in the body.
137
What happens if fat-soluble vitamins are consumed in excess?
Can lead to toxicity.
138
What are water-soluble vitamins?
B-complex and C; not stored significantly and must be regularly consumed.
139
What happens to excess water-soluble vitamins?
Readily excreted in urine.
140
What is the function of B vitamins?
Act as coenzymes in energy metabolism.
141
What are minerals?
Inorganic elements with diverse functions. ## Footnote minerals nutrition
142
Name some important minerals.
Phosphorus, potassium, sodium, zinc, and selenium. ## Footnote minerals nutrition
143
What are enzymes?
Enzymes are protein catalysts that increase the rate of chemical reactions without being changed in the overall process. ## Footnote biology enzymes
144
What is the primary role of an enzyme?
To lower the activation energy required to initiate a reaction by creating a more favorable reaction pathway. ## Footnote biology enzymes
145
What is the purpose of enzymes in biochemical reactions?
To lower the activation energy required to initiate a reaction by creating a more favorable reaction pathway.
146
How much faster can enzyme-catalyzed reactions occur compared to uncatalyzed reactions?
Enzyme-catalyzed reactions can process 10^3 to 10^11 times faster.
147
What is the protein nature of enzymes?
Almost all enzymes are globular proteins, except for some catalytic RNA molecules called ribozymes.
148
What is enzyme specificity?
Enzymes are highly specific, interacting with only one or a few substrates and catalyzing one type of chemical reaction.
149
What is the efficiency of enzymes?
Enzymes significantly increase the rate of biochemical reactions, making them essential for life.
MBS Biochemistry
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