Biological Molecules Flashcards

(61 cards)

1
Q

Monomers -> Polymers

A

Condensation

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2
Q

Polymers -> Monomers

A

Hydrolysis

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3
Q

Sugars and starches:

A

Energy sources

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4
Q

Cellulose and chitin:

A

Structural components

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5
Q

Glucose

A

Metabolic fuel

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6
Q

Sucrose

A

Table sugar

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7
Q

Glycogen, starch

A

Fuel stores

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8
Q

Glucose:

A

*most abundant monosaccharide
*hexose
*energy source
*synthesizes amino acids and fatty acids
*failure to keep constant: diabetes mellitus

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9
Q

Glycosidic bond

A

C-O-C

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10
Q

O-glycosidic bond

A

Anomeric/stereocenter carbon (C bonded to O and OH)

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11
Q

Maltose bond

A

Glucose-α(1-4)-glucose

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12
Q

Sucrose bond

A

Glucose-α(1-2)-fructose

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13
Q

Lactose bond

A

Galactose-β(1-4)-glucose

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14
Q

Sucrose:

A

*common table sugar
*hydrolyzed by invertase
Invertase is found in the inner walls of small intestine

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15
Q

Maltose:

A

Homodimer of glucose, by-product of starch hydrolysis

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16
Q

Lactose hydrolysis:

A

Lactase (human)
β-galactosidase (bacteria)

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17
Q

Lactose intolerance leads to

A

*Lactase deficiency
*Lactose accumulation in ileum
*Osmotic events

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18
Q

Polysaccharides -> Monosaccharides

A

Enzymatic or acid hydrolysis

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19
Q

Polysaccharides:

A

Homo (single type of monomer) or Hetero (many types of monomers)

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20
Q

Homopolysaccharides branch into:

A

Glucans (made from D-glucose)
e.g: starch, glycogen, cellulose
Mannans (made from mannons)

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21
Q

Heteropolysaccharides example:

A

Hyaluronic acid
Gives elastoviscosity to liquid connective tissues

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22
Q

Glycogen:

A

Branched biopolymer
Branches every 8-12 alpha glucose

Bond: (1,4)
Branches: (1,6)

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23
Q

Starch composition:

A

20% alpha-amylose
80% amylopectin

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24
Q

α-amylose:

A

Unbranched, long, (1,4) bonds

Not water soluble, forms micelles

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25
Micelles:
Hollow spherical structures that are hydrophobic inside and hydrophilic outside Their polymers form helical coils due to hydrogen bonding
26
Amylopectin:
Branch every 24-30 glucose Bond: (1,4) Branches: (1,6)
27
Amyloplasts =
Starch granules (store starch)
28
Hydrolysis of starch:
α-Amylase enzyme: saliva & pancreatic juices break α(1-4) bonds to produce glucose and maltose mix β-Amylase enzyme: malt (germinated cereal grain), yeasts, bacteria and moulds digest starch, glycogen + other polysaccharides' α(1-4) bonds break maltose units from non-reducing polymer end
29
α- and β-amylases degrade amylopectin
into dextrins, final product = limit dextrin debranch by isomaltase (or α-dextrinase)
30
Cellulose:
*most abundant carbohydrate *β(1-4) bonds *only provides fiber in the diet
31
Chitin:
monosaccharides have an -OH (hydroxyl group) replaced by an -NH2 (amino group) if monosaccharide is glucose, it forms glucosamine subunits are N-acetyl glucosamine
32
Glycosylation:
COVALENT addition of sugars to amino acids
33
Glycoproteins:
Oligosaccharides in glycosidic linkage to serine,threonine,asparagine amino acids
34
Phosophorylated sugars are:
1. anionic (-) 2. reactive intermediates in glycosidic bonding
35
Proteins role:
Structural components *Growth *Repair *Maintenance Controls what a cell looks like and how it functions
36
Classes of proteins:
-Enzymes -Structural (collagen, keratin) -Storage (ovalbumin, zein) -Transport (hemoglobin, membrane proteins) -Regulatory (kinases eg: insulin) -Motile (actin, myosin) -Protective (antibodies)
37
Amino acids to memorize
Glycine, R-group = H Alanine, R-group = CH3 Cysteine, R-group = CH2SH
38
Number of common amino acids
20
39
Polar R groups:
acids, amines, amides, alcohols acidic R : acidic amino acid amine R : basic amino acid examples: asparagine, serine, threonine, tyrosine, glutamine acids -> aspartic, glutamic basic -> arginine, lysine, histidine
40
Non-polar R groups:
Hydrocarbon alkyl groups (alkane branches) or Aromatic (benzene rings) examples: valine, alanine, phenylalanine, leucine, isoleucine
41
Protein structures:
Primary - peptide (C-N) Secondary - hydrogen bonding Tertiary - hydrogen, ionic, hydrophobic (weak), covalent/disulfide (strongest interactions, e.g: cysteine) Quaternary - same bonds as tertiary It is only when the protein has folded to its tertiary structure that it is able to function.
42
Alpha helix:
*About 11 AAs *Basic structural unit of some fibrous proteins *Provides elasticity (unwinding of coil, breaking of H-bonds)
43
Beta pleated sheet:
*Strong, flexible, not elastic, distance's fixed by strong covalent bonds *Example: protein of silk fibroin
44
Molecular Chaperones:
Catalyze (help) the folding of proteins Examples: Hsp70, Hsp60, Hsp90
45
Sickle cell anemia:
Single amino acid substitution in Beta-chains (polar glutamic acids changes to non-polar valine)
46
Denaturation:
Hydrogen and ionic bonding disruption Unfolding of chains
47
Groups of lipids:
Fats Phospholipids Carotenoids Steroids Waxes Prostaglandins
48
Function of lipids:
* Hormones (leptin, appetite suppressor) * Energy storage * Structural components (phospholipids) * Heat insulation * Shock absorption (in kidneys) * Vision (carotenoids) * Buoyancy
49
Fat =
Triglyceride = Triacylglyceride Monoacylglyceride -> Diacylglyceride -> Triacylglyceride (condensations) Diacylglycerol is an important molecule for sending signals within the cell
50
Saturated fatty acids:
Maximum number of hydrogen atoms, no double bonds Unhealthy solid at RT Example: Palmitic No dietary requirements
51
Unsaturated fatty acids:
Healthy, liquid at RT Some acids must be obtained from food: Linoleic (omega-6) : meat Lionelenic (omega-3) : fish+seeds Arachidonic : meat, fish and eggs Mono-unsaturated (only one double bond) example: oleic acid Poly-unsaturated (more than one double bond) example: linoleic acid
52
Phospholipids:
Diacylglycerol (two fatty acids) + phosphate Amphipathic Tail: two fatty acids Head: glycerol-phosphate-organic group
53
Carotenoids:
Red, orange and yellow plant pigments (play a role in photosynthesis) Converted to vitamin A Vitamin A: -growth and development, immunity -converted to retinal in cones and rods' light reception of mollusks, insects and vertebrates -deficiency leads to night blindness Caretenoids, vitamin A and retinal have 5-C monomers known as isoprene units with a pattern of alternating double and single bonds
54
Steroids:
4 rings 3 of which are 6 carbon, 1 is 5 carbon Form isoprene units as well *Length and structure of the side chains distinguish steroids
55
Steroid hormones:
Testosterone (natural) Stanozolol (synthetic)
56
Waxes:
Fatty acids bound to alcohol Solids at room temperatures
57
Nucleic acids:
DNA composes genes, two nucleotide chains held by hydrogen bonds RNA codes for amino acid sequence, one nucleotide chain made of: Five-carbon ring Phosphates (for acidity) Nitrogenous base (double bonds purine and single bonds pyrimidine)
58
Nitrogenous bases:
Cytosine + Adenine have a NH2 branch Guanine + Thymine + Uracil have a O branch, thymine has a CH3 side branch
59
Nucleic acid orientation:
5' to 3'
60
Strand orientation:
Template : 5' to 3' Non-template : 3' to 5'
61
Nucleotides examples:
ATP, cyclic AMP, cyclic GMP, NAD, NADH