biological molecules Flashcards

(42 cards)

1
Q

monomer

A

small repeating molcules which form larger molecules

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2
Q

polymer

A

Molecules made from many small identical monomers

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3
Q

condensation

A

2 molecules join
form chemical bond
releasing a water molecule

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4
Q

Monosaccharides

A

monomers from which larger carbs are made
glucose fructose and galactose

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5
Q

disacharide

A

2 monosaccharides joined by glycosidic bond
formed by condensation releasing water molecule

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6
Q

starch

A

energy store in plant cells
polysach of alpha glucose
1-4 GB unbranched amylose
1-4 1-6 GB branched amylopectin
helical so compact for storage in cell
large and insoluble cant leave cell
insol so wp unaffected

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7
Q

glycogen

A

energy store in animal cells
1-4 1-6 GB branched
made of alpha glucose
large and insoluble cant leave cell
insol so wp unaffected
branched so fit more molecules in small area
branched more ends for hydrolysis release glucose for respiration make ATP for energy release

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8
Q

Cellulose

A

strength and strucutral support to algal and plant cell walls
polysach of B glucose
1-4 straight unbranched chains
chains linked in parallel by h bonds forming microfibrils
every other b glucose inverted long straight unbranched chain
many h bonds link parallel strands strong fibres

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9
Q

test for reducing sugars

A

monosach maltose lactose
add bendicts blue to sample
heat in boiling water bath
pos result red ppt

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10
Q

non reducing test

A

sucrose
benedicts as above stays blue
heat in boiling water bath with acid to hydrolyse to red sugar
neut with alkali
heat in boiling water bath with benedicts
red ppt positive result

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11
Q

test for starch

A

add iodine dissolved in potassium iodide
shake stir
orangey brown to blue black

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12
Q

sat vs unsat fatty acid

A

sat no c=c db
unsat one or more c=c db

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13
Q

triglyceride formation

A

1 glycerol molecule
3 fatty acids
3 condensation reactions
removing three water molecules and forming 3 ester bonds

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14
Q

difference between phospholipid and triglycerides structure

A

one of the fatty acids is replaced by a phosphate containing group

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15
Q

phospholipid property to structure

A

form bilayer in cell memb allowing passage of small molcules and lipid soluble substances
phosphate head hydrophillic and attract to water
fatty acid tail hydrophobic repel water poiny away

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16
Q

lipid test

A

add ethanol
shake
add water
milky white emulsion

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17
Q

Explain how the properties of triglycerides are related to their structure

A

High ratio of C-H bonds to carbon atoms in hydrocarbon chain
so used in respiration to release more energy than the same mass of carbohydrates
non-polar fatty acids so insoluble in water
So no effect on water potential of cell

18
Q

Describe how amino acids join together

A

Condensation reaction
Removing a water molecule
COOH group of one
and amine / NH2 group of another
● Forming a peptide bond

19
Q

Describe the primary structure of a protein

A

Sequence of amino acids in a polypeptide chain, joined by peptide bonds

20
Q

secondary structure

A

Folding of polypeptide chain
alpha helix / beta pleated sheets
Due to hydrogen bonding between amino acids
● Between NH (group of one amino acid) and C=O (group)

21
Q

tertiary

A

3D folding of polypeptide chain
● Due to interactions between amino acid R groups
● Forming hydrogen bonds, ionic bonds and disulfide bridges

22
Q

quaternary

A

More than one polypeptide chain
Formed by interactions between polypeptides
(hydrogen bonds, ionic bonds, disulfide bridges)

23
Q

protien test

A

beirut reagent
purple colour

24
Q

Describe the induced-fit model of enzyme action

A

Substrate binds to (not completely complementary) active site of enzyme
2. Causing active site to change shape (slightly) so it is complementary to its substrate
3. So enzyme-substrate complex forms
4. Causing bonds in substrate to bend / distort, lowering activation energy

25
explain specificty of enzymes
Specific tertiary structure determines shape of active site ○ Dependent on sequence of amino acids (primary structure) ● Active site is complementary to a specific substrate ● Only this substrate can bind to active site, inducing fit and forming an enzyme-substrate complex
26
competitive inhibitor
As concentration of competitive inhibitor increases, rate of reaction decreases ○ Similar shape to substrate ○ Competes for active site ○ So substrates can’t bind ○ So fewer enzyme-substrate complexes form Increasing substrate concentration reduces effect of inhibitors
27
non comp inhibitor
● As concentration of non-competitive inhibitor increases, rate of reaction decreases ○ Binds (allosteric site) ○ Changes enzyme tertiary structure / active site shape ○ So active site no longer complementary to substrate ○ So substrates can’t bind ○ So fewer enzyme-substrate complexes form ● Increasing substrate concentration has no effect on rate of reaction as change to active site is permanent
28
dna
holds genetic info which codes for polypeptides thymine deoxyribose
29
rna
transfers genetic info from Dna to ribosomes uracil ribose
30
how do nucletodies join to form polynucleotides
Condensation reactions, removing water molecules ● Between phosphate group of one nucleotide and deoxyribose / ribose of another ● Forming phosphodiester bonds
31
Describe the structure of DNA
Polymer of nucleotides ● Each nucleotide formed from deoxyribose, a phosphate group and a nitrogen-containing organic base ● Phosphodiester bonds join adjacent nucleotides ● 2 polynucleotide chains held together by hydrogen bonds ● Between specific complementary base pairs - adenine / thymine and cytosine / guanine ● Double helix
32
structure of mrna
● Polymer of nucleotides (polynucleotide) ● Each nucleotide formed from ribose, a phosphate group and a nitrogen-containing organic base ● Bases - uracil, adenine, cytosine, guanine ● Phosphodiester bonds join adjacent nucleotides ● Single helix
33
dna s 2 f
● Two strands → both can act as templates for semi-conservative replication ● Hydrogen bonds between bases are weak → strands can be separated for replication ● Complementary base pairing → accurate replication ● Many hydrogen bonds between bases → stable / strong molecule ● Double helix with sugar phosphate backbone → protects bases / hydrogen bonds ● Long molecule → store lots of genetic information (that codes for polypeptides) ● Double helix (coiled) → compact
34
process of semi conservatv replication
1. DNA helicase breaks hydrogen bonds between complementary bases, unwinding the double helix 2. Both strands act as templates 3. Free DNA nucleotides attracted to exposed bases and join by specific complementary base pairing 4. Hydrogen bonds form between adenine-thymine and guanine-cytosine 5. DNA polymerase joins adjacent nucleotides on new strand by condensation reactions 6. Forming phosphodiester bonds
35
why does dna polymerase move in opposite directions
● DNA has antiparallel strands ● So shapes / arrangements of nucleotides on two ends are different ● DNA polymerase is an enzyme with a specific shaped active site ● So can only bind to substrate with complementary shape (phosphate end of developing strand)
36
atp strucutre
Ribose bound to a molecule of adenine and 3 phosphate groups ● Nucleotide derivative
37
how is atp broken down
● ATP (+ water) → ADP (adenosine diphosphate) + Pi (inorganic phosphate) ● Hydrolysis reaction, using a water molecule ● Catalysed by ATP hydrolase (enzyme)
38
Give two ways in which the hydrolysis of ATP is used in cells
● Coupled to energy requiring reactions within cells (releases energy) ○ eg. active transport, protein synthesis ● Inorganic phosphate released can be used to phosphorylate (add phosphate to) other compounds, making them more reactive
39
how is atp resyntheissed
● ADP + Pi → ATP (+ water) ● Condensation reaction, removing a water molecule ● Catalysed by ATP synthase (enzyme) ● During respiration and photosynthesis
40
how is atp a suitable immediate energy source
● Releases energy in (relatively) small amounts / little energy lost as heat ● Single reaction / one bond hydrolysed to release energy (so immediate release) ● Cannot pass out of cell
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