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Alevel Biology year 1 > Biological molecules > Flashcards

Biological molecules Flashcards

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1
Q

+what is a carbohydrate

A

molecule contains only C,H,O single unit called monosaccharide, 2 disaccharide and polysaccharide

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2
Q

What is glucose

A

Alpha and Beta glucose are hexose sugars
-many OH groups so is soluble in water

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3
Q

what is cytosol

A

fluid part of the cytoplasm

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4
Q

how does glucose bond

A

condensation reaction between 2 glucose molecules 2 OH groups react forming water and joins molecules by the O
1,4 glyosidic bond

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5
Q

What are the other sugars

A

fructose + glucose = sucrose
galactose + glucose = lactose

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6
Q

what are the pentose sugars

A

ribose and deoxyribose

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7
Q

what are the two variations of the polysaccharide starch

A

amylose, amylopectin

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8
Q

amylose

A

1,4 glyosidic bonds
bond angles cause a helix shape to form supported by H bonds
compact and less soluble than glucose

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9
Q

amylopectin

A

1,4 and 1,6 glyosidic
causes branches
more compact
less soluble
1,6 bond every 25 glucose subunits

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10
Q

glycogen

A

animal storage unit
more branches so more compact and less space required to store it
animals are more metabolically active so neccessary
branching allows for glucose to easily be added to removed

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11
Q

what is hydrolysis

A

turned stored nutrients into usable energy
water, enzymes used to break down molecules

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12
Q

cellulose

A

beta glucose
rotates in 180degrees so the OH groups can interact with each other, causes long straight chain molecules

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13
Q

how does cellulose make fibres

A

cellulose chains make H bonds which form microfibrils many of the microfibrils come together to make microfibrils which come together to make fibres which are strong and insoluble

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14
Q

what is the test for reducing sugars and why

A

CU(II)SO4-2 has a blue colour when reducing sugar is added to the solution the CU(II)SO4-2 is reducing causing it to change colour from blue to red .
Heat in copper sulphate solution and red ppt should form as a layer depending on reducing sugar conc

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15
Q

Test for non reducing

A

Boil the solution in HCL to break down the sugars then add an alkali solution to neutralise it. Then do a normal test for reducing sugars red-blue
Disaccharide/ polysaccharide should be broken down into a monosaccharide

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16
Q

What is the test for Starch

A

Add iodine dissolved in potassium iodide solution should go from yellow/brown to purple/black

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17
Q

What are lipids

A

C,O,H mainly
fats are solid lipids RTP
oils are lipids that are liquid RTP

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18
Q

What is a triglyceride

A

1 glycerol group 3 fatty acids, forms ester bonds(esterification)
3 water molecules required to break it down

19
Q

saturated/unsaturated meaning

A

sat- no double bonds, all bonds possible by H are made
unsat- double bonds

20
Q

Phospholipids

A

modified triglycerides 2 fatty acids 1 glycerol and one phosphate group( many electrons so it is hydrophilic)

21
Q

What is a sterol

A

complex alcohols, 4 ring structure with an OH group at the end
amphiphilic

22
Q

cholesterol

A

made in liver/ intestines
between phospholipids stops them getting rigid at low temps and fluid at high ones

23
Q

roles of lipids

A

hydrophobic barriers
hormone production
electrical insulation
waterproof

24
Q

roles of triglycerides

A

long term energy store
cushioning(protects organs)
buoyancy for aquatic animals

25
Q

what is the test for lipids

A

ethanol + water shake and positive result is white emulsification

26
Q

amino acids

A

same basic structure with differing R groups

27
Q

types of Amino acid

A

5 are non essential and are made from other a.a
9 are essential and obtained from what we eat
6 are only needed in early development

28
Q

Peptide bond

A

H on one of the Amine groups and and OH of the carboxylic groups bond forming peptide bond and water

29
Q

what enzyme catalyses the bonding of peptides

A

peptidyl transferase(in ribosomes)

30
Q

primary structure of amino acid

A

sequence of amino acids, directed by DNA. The sequence influences how the chain folds to give it its function and shape.

31
Q

secondary structure of amino acid

A

O, H, N atoms interact causing H bonds to form in the chain pulling it into a alpha helix shape, peptide chains forming parallel to each other form H bonds forming a beta pleated sheet

32
Q

tertiary structure of amino acid

A

folding of protein into its final shape, causes R groups to interact with each other
hydrophobic/ hydrophilic interactions
H bonds weakest bond
ionic bonds form from opposite charged R groups
disfulide bonds- form between two sulphur atoms

33
Q

quaternary structure of amino acid

A

Two or more proteins working together(subunits) same interacts but between subunits
subunits can be different or identical
enzymes have 2 identical subunits

34
Q

polar/ non polar interactions

A

proteins fold so that the hydrophilic R groups are pointed outwards toward the aqueous environment

35
Q

breakdown of peptides

A

Protease catalyses reverse reaction of peptides, water molecule used to break peptide bond reforming Amine group and COOH

36
Q

Globular proteins

A

compact, soluble and spherical
polar R groups are on the outside makes it soluble
solubility is important for functions

37
Q

insulin

A

regulation of blood glucose, transported in blood stream so needs to soluble, need to fit on specific receptors so need a specific A,A chain

38
Q

Conjugated proteins

A

globular proteins with a non protein component(prosthetic group)
Haem group in the blood made of Fe2+ which can reversibly bind to O2 to move it around the body from lungs to cells
haemoglobin made from 2 alpha and 2 beta units

39
Q

catalase

A

enzyme with specific reaction type, quaternary with 4 haem groups, Fe2+ react with hydrogen peroxide(metabolism by-product and speed up its breakdown)

40
Q

fibrous proteins

A

long insoluble molecules, many hydrophobic R groups in primary structure. small range of amino acids and repetitive

41
Q

Elastin

A

found in elastic fibres, (walls of blood vessels) need to be flexible, return to normal, quaternary protein made of tropoelastin
cross links of covalent bonds

42
Q

Keratin

A

hair , skin, nails
large amount of sulphur containing a.a cysteine. forms strong disulphide bridges pending on the amount of bridges the flexibility varies

43
Q

Collagen

A

skin, tendons and ligaments. 3 polypeptide chain wound in a rope like structure still flexible
every third a.a is glycine which makes the allows the protein to form packed helix. H bonds between polypeptide chains long quaternary proteins with staggered ends

Alevel Biology year 1 (14 decks)

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