Biological molecules Flashcards

(43 cards)

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
what is the test for lipids
ethanol + water shake and positive result is white emulsification
26
amino acids
same basic structure with differing R groups
27
types of Amino acid
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
Peptide bond
H on one of the Amine groups and and OH of the carboxylic groups bond forming peptide bond and water
29
what enzyme catalyses the bonding of peptides
peptidyl transferase(in ribosomes)
30
primary structure of amino acid
sequence of amino acids, directed by DNA. The sequence influences how the chain folds to give it its function and shape.
31
secondary structure of amino acid
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
tertiary structure of amino acid
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
quaternary structure of amino acid
Two or more proteins working together(subunits) same interacts but between subunits subunits can be different or identical enzymes have 2 identical subunits
34
polar/ non polar interactions
proteins fold so that the hydrophilic R groups are pointed outwards toward the aqueous environment
35
breakdown of peptides
Protease catalyses reverse reaction of peptides, water molecule used to break peptide bond reforming Amine group and COOH
36
Globular proteins
compact, soluble and spherical polar R groups are on the outside makes it soluble solubility is important for functions
37
insulin
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
Conjugated proteins
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
catalase
enzyme with specific reaction type, quaternary with 4 haem groups, Fe2+ react with hydrogen peroxide(metabolism by-product and speed up its breakdown)
40
fibrous proteins
long insoluble molecules, many hydrophobic R groups in primary structure. small range of amino acids and repetitive
41
Elastin
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
Keratin
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
Collagen
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