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Bellas Biology > Topic 1.2 Biological Molecules > Flashcards

Topic 1.2 Biological Molecules Flashcards

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1
Q

What is a glycosidic bond?

A

A bond formed between two monosaccharides (1,4 or 1,6).

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2
Q

Amylose

A

-One of the 2 polysaccharides that make up starch
-Long
-Unbranched
-Coiled structure (makes it compact)
(Starch- alpha helix structure, insoluble due to its structure).

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3
Q

Hydrophilic

A

-Having an affinity for water
-Capable of interacting with water through hydrogen bonding.

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4
Q

Hydrophobic

A

-Lacking an affinity for water
-Insoluble in water
-Repelling water
-Doesn’t form hydrogen bonds.

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5
Q

Is a lipid a polymer?

A

NO
-It is only 3 chains long, not repeated.

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6
Q

What do lipids contain?

A

-Carbon
-Hydrogen
-Oxygen
-Phosphorous (sometimes)
-Nitrogen (sometimes).

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7
Q

Cellulose properties

A

Occurs in: plants
Location: cell wall
Monomer: beta glucose
Glycosidic bond: 1-4
Shape of chains: very long and straight
Hydrogen bonds: extensive
Tensile strength: high
Function: structural and protective.

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8
Q

What is a condensation reaction?

A

A reaction that joins two monosaccharides (a molecule of water is produced).

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9
Q

What is a hydrolysis reaction?

A

A reaction that splits the disaccharide back into its monomer (using a molecule of water).

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10
Q

Glycerol structure

A

-Fats/lipids have a backbone of glycerol
-Fatty acids are hydrocarbon length
(structure ‘prop-1,2,3-anol : CH2OH CHOH CH2OH)
-Group: picture

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11
Q

Amylopectin

A

-One if the two polysaccharides that make up starch
-Long
-Branched; branches allow enzymes to break it down easily (by breaking glycosidic bonds) so glucose can be released quickly.

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12
Q

Glycogen properties

A

Occurs in: animals
Location: cytoplasm
Monomer: alpha glucose
Glycosidic bond:1-4 and 1-6
Shape of chains: coiled
Hydrogen bonds: limited
Tensile strength: low
Function: energy store.

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13
Q

Starch properties

A

Occurs in: plants
Location: chloroplasts, amyloplasts
Monomer: alpha glucose
Glycosidic bond: 1-4 and 1-6
Shape of change: coiled
Hydrogen bonds: limited number
Tensile strength: low
Function: energy store.

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14
Q

Cellulose

A

-Monomer is beta glucose
-Forms chains which run parallel with hydrogen bonds to form microfibrils
-Microfibrils are string
-Being fibrous cellulose is structurally important in plant cell walls.

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15
Q

Beta glucose structure

A

(Ballerina- ‘one arm up one arm down’)
trans isomer

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16
Q

Proteins equation

A

protein + water ⇌ amino acids

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17
Q

Ester bond

A

Bond between fatty acids and glycerol.

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18
Q

Condensation reaction for lipid

A

Glycerol + fatty acid –> lipid
(eliminating three H2O molecules).

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19
Q

Phospholipid

A

Phosphate group head (hydrophilic)
Fatty acid tail (hydrophobic)

20
Q

Alpha glucose structure

A

(Acrobat- ‘moustache’)
cis isomer
(small and water soluble)

21
Q

Test for triglycerides

A

Emulsion test
-water (shake) + ethanol (shake).

22
Q

Functions of proteins and examples

A

-Channels eg. membrane proteins
-Hormones eg. insulin
-Transport eg. haemoglobin
-Protection eg. antibodies
-Structure eg. collagen, keratin
-Cell recognition eg. antigens
-Movement eg. actin, myosin

23
Q

Amino acid structure

A
24
Q

Peptide bond

A

A peptide bond is a bond between two amino acids, formed by a condensation reaction

25
Q

Polyunsaturated

A

Molecules that contain more than one unsaturated carbon bond.

26
Q

Peptide bond

A

A bonds between 2 polypeptides (amino acid).

27
Q

Tertiary structure (3°)

A

-Protein folds tightly
-Held together by bonds between R groups (disulphide bonds, hydrogen bonds, ionic bonds).

28
Q

Secondary structure (2°)

A

-Interactions between side chains cause chains to coil and twist
-Secondary structure is held together by hydrogen bonds
-Alpha helix and beta pleated sheets

29
Q

Phospholipid structure

A

Amphipathic: glycerol backbone attached to 2 hydrophobic fatty acid tails (by ester bonds) and a hydrophilic polar phosphate head.
(Tails can splay outwards= waterproofing)

30
Q

Primary structure (1°)

A

-Sequence/order of amino acids
-Link by peptide bonds in condensation reactions
-A polypeptide forms.

31
Q

Quaternary structure (4°)

A

-Several folded units join together
-Held together by bonds including those that form between R groups and adjacent chains (disulphide bridges).

32
Q

Glycerol/glycolipid structure

A

picture

33
Q

Monosaccharides

A

Organic monomer that cannot be hydrolysed to a simpler sugar.
3 hexose monosaccharides: glucose, fructose, galactose

34
Q

Structure of ribose

A

Pentose monosaccharide

35
Q

Disaccharide examples

A

-Maltose: glucose + glucose
-Sucrose: glucose + fructose
-Lactose: glucose + galactose
(all have formula C12H22O11)

36
Q

Polysaccharide definition

A

Polymer made from a repeating monosaccharide unit
-Starch
-Glycogen
-Cellulose

37
Q

How do triglycerides form?

A

Condensation reaction between 1 molecule of glycerol and 3 fatty acids form ester bonds.

38
Q

Saturated fatty acids

A

-Contain only single bonds
-Straight-chain molecules have many contact points
-Higher melting point= solid at room temperature
-Found in animal fats

39
Q

Unsaturated fatty acids

A

-Contain C=C double bonds
-‘Kinked’ molecules have fewer contact points
-Lower melting points= liquid at room temperature
-Found in plant oils

40
Q

Disulphide bridges in tertiary structure

A

Strong covalent S-S bond between molecules of the amino acid cysteine.

41
Q

Ionic bonds in tertiary structure

A

Relatively strong bonds between charged R groups.
(pH changes causes these bonds to break due to interactions with OH- / H+ ions).

42
Q

Hydrogen bonds in tertiary structure

A

Intermolecular force between H δ+ of O-H or N-H and lone pair on O or N of an adjacent molecule.
Numerous and easily broken.

43
Q

Structure and function of globular proteins

A

-Spherical and compact
-Hydrophilic R groups face outwards and hydrophobic R groups face inwards= usually water-soluble.
-Involved I metabolic processes eg. enzymes

44
Q

Structure and functions of fibrous proteins

A

-Can form long chains or fibres
-Sequences of amino acids repeat
-Insoluble in water
-Useful for structure and support eg. collagen.

45
Q

Functions of collagen

A

Component of bones, cartilage, connective tissue, tendons.

46
Q

Structure of collagen

A

-Stable alpha helix due to repeating sequence
-Forms fibres
-H bonds and staggered covalent bonds between fibres= high tensile strength.

47
Q

Structure of a globular protein

A
  • Has a tertiary structure and quaternary structure.
  • Held by named bond.
  • Hydrophilic on the outside of the molecule.

Bellas Biology (34 decks)

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