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module 2 > Biological Molecules > Flashcards

Biological Molecules Flashcards

1
Q

Bond formed and polymer for
Amino acids
Nucleotide
Monosaccharides

A

Amino acids - peptide bond, form proteins (polypeptides)
Nucleotide - phosphodiester bond, forms nucleic acids (RNA, DNA)
Monosaccharides - glycosidic, polysaccharides

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2
Q

Constituent elements of
Carbohydrates
Proteins
Lipids
Nucleic acids

A

Carbs - CHO (more O, less H)
Proteins - CHONS
lipids - CHO (more H, less O)
Nucleic - CHONP

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3
Q

Water is a […] molecule

A

Polar

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4
Q

Formation of H bonds in water

A
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5
Q

Properties and roles of water

A

+ solid ice = less dense than water (l) therefore surface of ice = habitat for organisms
Water beneath ice remains insulated and aquatic organisms don’t freeze to death

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6
Q

Alpha vs beta glucose

A
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7
Q

3 diff disaccharide we have to know

A

Maltose
Sucrose
Lactose

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8
Q

Constituents of the 3 disaccharides

A

a gluc + a gluc -> maltose & water (1,4 bonds)

a gluc + fruc-> sucrose & water (1,2 bond)

a gluc + b galactose -> lactose & water (1,4 bond)
Glycosidic bonds also form where the 2OH groups of separate monosaccharide are adjacent

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9
Q

Carbohydrate function

A

Energy store, energy source, structural units

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10
Q

Deoxyribose vs ribose

A
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11
Q

Deoxyribose vs ribose

A
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12
Q

Reducing vs non-reducing sugars

A
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13
Q

Starch features & function

A
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14
Q

Amylose vs amylopectin

A
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15
Q

Function of cellulose

A

Main structural constituent of plant cell walls

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16
Q

Features of cellulose

A
  • high tensile strength
  • insoluble in water
  • flexible
  • strong microfibrils
  • fibrous
  • not granular
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17
Q

Cellulose structure details

A

-b glucose monomers 1,4 glycoside bonds

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18
Q

Why are branched polysaccharides better for energy storage

A
  • lots of branches for enzymes to attach to
  • compact molecules
  • high energy content for their mass
  • can quickly be hydrolysed
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19
Q

What is glycogen

A

Main energy storage polysaccharide found in animals and fungi

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20
Q

Why is glycogen better than amylopectin etc

A

Forms more branches than it so more compact
In animals as it’s Better for storage = more useful for MOBILE animals

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21
Q

Glycogen structure

A
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22
Q

Lipid characteristics

A
  • macromolecules
  • non polar
  • have a chain of carbon atoms as a backbone
  • insoluble in water
  • soluble in alcohol
23
Q

Saturated vs unsaturated lipids

A

Unsaturated = double bonds in C=C

24
Q

Effect of double bond in unsaturated lipids

A

Causes molecule to bend / kink
So less able to pack tighter nicely, therefore dense
So b.p. Less

25
Q

How are triglycerides formed from 1 glycerol & 3 fatty acids

A
26
Q

Glycerol + fatty acid structure

A
27
Q

Functions of triglycerides

A
28
Q

What are phospholipids

A

Modified triglycerides
One fatty acid change replaced by inorganic phosphate ion (PO4)3-

29
Q

Phospholipids made up of?
And function

A

Form selective permeable phospholipid bilayer
Made up of 1 glycerol, 2 fatty acids & a phosphate group therefore polar

30
Q

Phospholipids in water? E.g. how does hydrophobia & philia play a role

A
31
Q

What roles of the phospholipid bilayer are there?

A

Forms the cell membrane,
(which plays a role in Compartmentalisation: to separate the sites of chemical reactions and allow for the formation of concentration gradients)

Separate as the cytoplasm from outer (aq) environments

32
Q

What are sterols and their function

A
33
Q

Roles of lipids

A

Membrane formation (hydrophobic barrier)
Hormone production
Electrical insulation (neuron myelin sheath).
Waterproofing (birth feathers, plant leaves)

34
Q

Lipid identification emulsion test steps

A
  1. Mix sample with ethanol (if solid should be ground up first)
  2. Mix solution with water & shake
  3. If the white emulsion forms @ top, indicator of lipid
35
Q

General structure of an Amino acid

A
36
Q

How peptide bond form

A
37
Q

Oligopeptide vs polypeptide

A

Oligo = short chain of amino acids linked together
Poly = long chain

38
Q

How many protein structures

A

4

39
Q

Protein primary structure

A

The sequence of amino acids in a polypeptide chain, specific to each protein

40
Q

Protein secondary structure

A

Formed due to hydrogen bonds forming between amine group and carboxylic group which leads to the folding into a beta pleated sheet or coiling into an alpha helix
H bond can be broken at high temps & pH changes

41
Q

Tertiary structure + types of bonds formed in it

A

The further coiling and folding of the amino acid to form the overall 3D shape of a protein & additional bonds being formed between R groups
Hydrogen - between R groups = weakest bind
Ionic - between pos & neg R groups
Disulfide (strong cov bonds between 2 cysteine R groups (these contain S atoms & can be broken by oxidation)
Weak hydrophobic interactions - between non-polar, hydrophobic R groups, to cause twisting of amino acid chains

42
Q

Quaternary structure of proteins

A

Consisting of many polypeptide chains
Contains b and alpha subunits & peptide bonds
The arrangement of 2nor more polypeptide chains in a protein make up its quaternary number

43
Q

Types of proteins

A

Globular & fibrous

44
Q

Globular protein features / structure / function

A
45
Q

Examples of globular proteins and what they do

A
46
Q

What are conjugated proteins + example

A

Haemoglobin

47
Q

Haemoglobic structure & function

A
48
Q

Fibrous protein features

A
49
Q

3 examples of fibrous proteins?

A

Keratin
Elastins
Collagen

50
Q

Keratin function

A

Provides mechanical protection & is waterproof
Impermeable barrier to infection
Found in nails and hair

51
Q

Elastins function

A

Allows stretch and recoil in lungs
+ in blood vessels to maintain blood pressure

52
Q

Collagen function and structure

A

Provides mechanical strength:
Withstands arteries high pressure
Tendons & binds made of collagen
Connective tissue

Structure
Every 3rd amino acid = glycine = allows polypeptide chain closeness
Formed of 3 polypeptide chains with H bonds between them, forming a triple helix
Adjacent molecules joined by cross links which are staggered in the ends of fibrils

53
Q

Give 3 functions of the cytoskeleton

A

Hold organelles in place
Provide strength & support (not structural)
Movement of chromosomes

module 2 (12 decks)

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