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FUNBIO > Biological Molecules > Flashcards

Biological Molecules Flashcards

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
Q

Micelles:

A

Hollow spherical structures that are hydrophobic inside and hydrophilic outside

Their polymers form helical coils due to hydrogen bonding

26
Q

Amylopectin:

A

Branch every 24-30 glucose
Bond: (1,4)
Branches: (1,6)

27
Q

Amyloplasts =

A

Starch granules (store starch)

28
Q

Hydrolysis of starch:

A

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
Q

α- and β-amylases degrade amylopectin

A

into dextrins,
final product = limit dextrin
debranch by isomaltase (or α-dextrinase)

30
Q

Cellulose:

A

*most abundant carbohydrate
*β(1-4) bonds
*only provides fiber in the diet

31
Q

Chitin:

A

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
Q

Glycosylation:

A

COVALENT addition of sugars to amino acids

33
Q

Glycoproteins:

A

Oligosaccharides in glycosidic linkage to serine,threonine,asparagine amino acids

34
Q

Phosophorylated sugars are:

A
  1. anionic (-)
  2. reactive intermediates in glycosidic bonding
35
Q

Proteins role:

A

Structural components
*Growth *Repair *Maintenance

Controls what a cell looks like and how it functions

36
Q

Classes of proteins:

A

-Enzymes
-Structural (collagen, keratin)
-Storage (ovalbumin, zein)
-Transport (hemoglobin, membrane proteins)
-Regulatory (kinases eg: insulin)
-Motile (actin, myosin)
-Protective (antibodies)

37
Q

Amino acids to memorize

A

Glycine, R-group = H
Alanine, R-group = CH3
Cysteine, R-group = CH2SH

38
Q

Number of common amino acids

A

20

39
Q

Polar R groups:

A

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
Q

Non-polar R groups:

A

Hydrocarbon alkyl groups (alkane branches) or Aromatic (benzene rings)

examples: valine, alanine, phenylalanine, leucine, isoleucine

41
Q

Protein structures:

A

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
Q

Alpha helix:

A

*About 11 AAs
*Basic structural unit of some fibrous proteins
*Provides elasticity (unwinding of coil, breaking of H-bonds)

43
Q

Beta pleated sheet:

A

*Strong, flexible, not elastic, distance’s fixed by strong covalent bonds

*Example: protein of silk fibroin

44
Q

Molecular Chaperones:

A

Catalyze (help) the folding of proteins

Examples: Hsp70, Hsp60, Hsp90

45
Q

Sickle cell anemia:

A

Single amino acid substitution in Beta-chains (polar glutamic acids changes to non-polar valine)

46
Q

Denaturation:

A

Hydrogen and ionic bonding disruption
Unfolding of chains

47
Q

Groups of lipids:

A

Fats
Phospholipids
Carotenoids
Steroids
Waxes
Prostaglandins

48
Q

Function of lipids:

A
  • Hormones (leptin, appetite suppressor)
  • Energy storage
  • Structural components (phospholipids)
  • Heat insulation
  • Shock absorption (in kidneys)
  • Vision (carotenoids)
  • Buoyancy
49
Q

Fat =

A

Triglyceride = Triacylglyceride

Monoacylglyceride -> Diacylglyceride -> Triacylglyceride (condensations)

Diacylglycerol is an important molecule for sending signals within the cell

50
Q

Saturated fatty acids:

A

Maximum number of hydrogen atoms, no double bonds
Unhealthy solid at RT
Example: Palmitic

No dietary requirements

51
Q

Unsaturated fatty acids:

A

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
Q

Phospholipids:

A

Diacylglycerol (two fatty acids) + phosphate
Amphipathic

Tail: two fatty acids
Head: glycerol-phosphate-organic group

53
Q

Carotenoids:

A

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
Q

Steroids:

A

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
Q

Steroid hormones:

A

Testosterone (natural)
Stanozolol (synthetic)

56
Q

Waxes:

A

Fatty acids bound to alcohol
Solids at room temperatures

57
Q

Nucleic acids:

A

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
Q

Nitrogenous bases:

A

Cytosine + Adenine have a NH2 branch

Guanine + Thymine + Uracil have a O branch, thymine has a CH3 side branch

59
Q

Nucleic acid orientation:

A

5’ to 3’

60
Q

Strand orientation:

A

Template : 5’ to 3’
Non-template : 3’ to 5’

61
Q

Nucleotides examples:

A

ATP, cyclic AMP, cyclic GMP, NAD, NADH

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