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Sport Science sem 1 > Biochem sem1 > Flashcards

Biochem sem1 Flashcards

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1
Q

What does the:
atomic number
atomic mass
Represent

A

Number: protons
Mass: protons and neutrons

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2
Q

what is the most common chemical formula for a monosaccharide?

A

(CH2o)n
n=3,5,6

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3
Q

What is the name of:
1 sacharide
2 sacharides
3-10 sacharides
10+ sacharides

A

1 = monosaccharide
2 = disaccharide
3 = ogliosaccharide
10+ = polysaccharide

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4
Q

How do multiple saccharides bond?

A

Through condensation reaction
glycosidic bond (type of ether bond)

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5
Q

what makes up
sucrose
lactose
maltose

A

sucrose = glucose + fructose
lactose = glucose + galactose
maltose = 2 alpha glucose

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6
Q

What is Van Der Waals?

A

cloud of - charge around atom, can congregate in one section to attract other atoms

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7
Q

What are 5 roles of lipids?

A
  • cell membranes
  • protection/insulation
  • neurone myelination
  • hormone production
  • absorb fat soluble vitamins
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8
Q

what are the 3 classifications of lipids?

A
  • triglycerides
  • phospholipids
  • sterols
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9
Q

Describe triglycerides?

A

TRIGLYCERIDES:
- glycerol backbone 3FA condensation reaction, sat (c-c) bonds or unsat (at least 1 c=c)
- double bond can be cis or trans

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10
Q

Describe phospholipids?

A

arranged in bilayers
hydrophilic tails
hydrophobic head

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11
Q

Describe sterols?

A
  • cyclic organic compound
  • found in most eukaryotic cells
  • e.g: cholesterol
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12
Q

what are proteinogenic amino acids?
What do they consist of?

A
  • only 20 genetically coded amino acids in DNA
  • amine group, carboxyl group, hydrogen atom, organic side chain (R group)
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13
Q

How and what is a protein formed of?

A

Peptide chains = amino acids joined by condensation reaction, peptide bond between carboxyl and amine groups

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14
Q

What is the primary structure?

A

amino acid sequence from N- terminus to C- terminus?

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15
Q

what is the secondary structure?

A

alpha helix =
- c=o forms H bond with amine hydrogen between carboxyl and amine group
- turns right handed

beta sheet =
- parallel or antiparallel structure
- zig zag peptide chain
- backbone forms H bonds between segments

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16
Q

what is the tertiary and quaternary structure?

A

Tertiary =
- a helix or b sheet folds itself, 3D, intermolecular forces change shape

Quaternary =
- multiple subunits
- intermolecular forces change behaviour

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17
Q

What is avogadros constant?

A

6.02 X 10^23

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18
Q

how do you calculate molarity?

A

mass of substance (g)

molecular| number of
weight | moles

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19
Q

what is a heterocyle?

A

ring that has another element in it

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20
Q

what are 3 regular classes of functional groups?

(draw them ideally)

A

hydroxyl
amine
carbonyl

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21
Q

what are the 2 laws of thermodynamics?

A

1 = energy cant be created or destroyed only interconverted between forms

2 = total entropy of a system always increases

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22
Q

what is entropy and enthalpy?

A

entropy = level of disorder
enthalpy = energy

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23
Q

what is the definition of Gibbs free energy?

A

the amount of available energy to do work

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24
Q

what is the equation for Gibbs free energy?

A

△G = △H-T △S

G= Gibbs free energy
H = enthalpy
T= temperature
S= entropy

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25
Q

When △G is more than zero reaction is?
When △G is less than zero reaction is?

A

More than 0 = not spontaneous (requires addition of energy to occur)

Less than 0 = spontaneous (happens on its own)

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26
Q

Explain what a coupled reaction is?

A

when an exergonic reaction drives an endergonic reaction

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27
Q

What is an:
anabolic reaction
catabolic reaction

A

anabolic = smaller — bigger

catabolic = bigger — smaller

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28
Q

What is energy stored as by activated carrier molecules?

A

transferable chemical group or electrons

instead of being lost as heat

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29
Q

when △S (entropy):
bigger than zero
less than zero
Entropy is ordered or disordered
?

A

bigger than zero = disordered

less than zero = ordered

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30
Q

how do cells get energy? where is the energy stored?

A

energy from oxidising organic molecules by metabolism

store in covalent bonds

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31
Q

explain REDOX?

A

Oxidation is loss of electrons

reduction is gain of electrons

32
Q

Describe haemoglobins structure

A

2 alpha subunits, 2 beta subunits
globular, compact
tetrameric protein
o2 binds to haem groups

33
Q

what are enzymes?

A
  • biological catalysts
  • regenerated at end of reaction so not used up
  • globular
  • powerful
34
Q

Name 5 biological functions enzymes are used in?

A
  • metabolism
  • movement
  • digestion
  • cell signalling
  • gene expression
35
Q

describe the structure of an enzyme?

A
  • globular protein
  • AA sequence decides catalytic activity
  • active site has different AA, some for binding substrate, some for catalysing reaction
36
Q

What are the two theories of enzyme binding?

A

LOCK AND KEY: rigid and fixed, complementary geometry

INDUCED FIT: conformational change in binding

37
Q

Describe the allosteric site?

A
  • can induce conformational change e.g: change in active site/ROR
  • regulatory molecule binds and inhibits/activate enzyme
38
Q

what is a:
- cofactor
- coenzyme
- prosthetic group

A

cofactor: inorganic, required for enzyme/protein to work

coenzyme: organic, directly involved in enzyme reaction, transiently bond, required for optimal

prothetic group: non protein molecule covalently bonds for enzyme function

39
Q

What is an enzyme called when It needs a cofactor/enzyme when:
- cofactor hasn’t bound?
- cofactor has bound?

A

Hasn’t bound: APOENZYME
Has bound: HOLOENZYME

40
Q

What enzyme? pt1
1. transfer H or O2 or E- from one substrate to another
2. transfer functional groups from one substrate to another
3. hydrolysis of a substrate

A
  1. oxidoreductases
  2. transferases
  3. hydrolases
41
Q

What enzyme? pt2
4. add or remove a group to form a double bond
5. transfer groups within a molecule
6. bond formation coupled with ATP hydrolysis

A
  1. lyases
  2. isomerases
  3. ligases
42
Q

what is:
1.activation energy
2. transition state

A
  1. energy barrier required to be overcome for reaction
  2. not substrate not product, transient molecular state
43
Q

9 ways which enzymes reduce activation energy?

A
  1. exclusion of water
  2. induced fit
  3. close proximity of substrate and enzyme
  4. metal ion cataylses
  5. covalent catalyses
  6. acid base catalyses
  7. chemical complementarity
  8. transition state stabilisation
  9. substrate binding and orientation
44
Q

describe the 4 main catalytic mechanisms

A
  1. metal ion catalyses: use metal ion to help with catalyses
  2. covalent catalyses: briefly substrate binds with covalent bond until substrate fully bonds
  3. enzyme transfers H to catalyses can occur
  4. approximation = further away is harder
45
Q

What is enzyme velocity?
When must it be measured

A
  1. initial ROR, amount of substrate covered to product per unit of time

Must be measured before 10% of substrate is converted

46
Q

What is VMax?
What is Km? How do you calculate it

A

Vmax = max enzyme ror
Km = measure of affinity for substrate to enzyme

also conc of substrate when 1/2 Vmax
1. Calc vmax, calc 1/2 vmax, draw line down to substrate conc

47
Q

what does…. indicate?
1. high Km
2. Low Km

A
  1. weak binding , need high substrate conc to reach Vmax
  2. strong bonding, need low substrate conc to reach vmax
48
Q

how to regulatory mechanism control enzyme activity?

A
  • allosteric inhibition/activation
  • confine enzymes into compartments
  • cell controls quantities of enzymes so is controlled
  • covalently modify to control activity
  • rate of protein destruction by targeted proteolyses
49
Q

describe 4 types of reversible inhibition?

how is Vmax effected for each?

A
  1. end product inhibition: end product inhibits earlier pathways
  2. competitive: inhibitor blocks actual substrate. Vmax = same, longer to get there
  3. non competitive: inhibitor binds to allosteric site, conformational change, Vmax lower
  4. uncompetitive: substrate already bound, inhibitor binds and stop catalysis. Vmax lower
50
Q

what is metabolism?

A

series of anabolic and catabolic reactions that happen in living cells

51
Q

Name 4 examples of catabolic reactions

A
  1. protein breakdown
  2. lipid oxidation
  3. carbohydrate oxidation
  4. nucleotide hydrolysis
52
Q

Name 4 examples of anabolic reactions

A
  1. protein synthesis
  2. lipid synthesis
  3. carbohydrate synthesis
  4. nucleotide synthesis
53
Q

if deltaG is large is ATP more or less willing to give up its phosphates?

A

more

54
Q

Where does lactate come from?

A

When no o2 present, anaerobic respiration uses glycolysis to produce ATP

NADH passes electrons to pyruvate to form lactate

55
Q

give 5 examples of membrane function

A
  1. chemical/physical barrier
  2. cell/cell communication
  3. energy conversion
  4. recognition
  5. allow cellular processes
56
Q

what is the word for: hydrophillic+hydrophobic parts?

A

amphipathic

57
Q

how can mutation in enzyme lead to disease?

A

over/under production , deletion leads to wrong enzymes created, regulate cell cycle = lead to cancers

58
Q

how is an enzymes structure specific to substrate?

A

amino acid sequence specifies 3D conformation
active site has different AA sequence
Cleft on surface of active site

59
Q

Describe the allosteric site

A

can induce conformational change
activate or inhibit reactions

60
Q

what is the standard unit of enzyme activity?

A

U

61
Q

how does temp effect enzyme activity?

A

rise = overcome activation energy, increase ror
too high = breaks bonds, alter active site, denature protein

62
Q

spontaneous or not?

1) △S﹥0 and △H < 0
2) △S﹥0 and △H﹥0
3) △S < 0 and △H < 0
4) △S < 0 and △H﹥0

A

1) spontaneous
2) spontaneous at high temp
3) spontaneous at low temps
4) not spontaneous

63
Q

what is the most important activated carrier molecule?

what reactions does it drive?

A

ATP

endergonic

64
Q

what is △G°

A

standard conditions, 25°c, 298K

65
Q

what is △G°’ (delta G nought prime)

A

standard biological conditions, 37°, 310K

66
Q

what do the different parts of this equation mean?
△G=△G° + RT ln Q

A

△G = change in gfe
△G° = delta g in standard conditions
R = 8.314J mol-1, K-1
T = temp
ln = log
Q = [products] / [reactants]

67
Q

with this reaction: △G=△G° + RT ln Q,
what do you do when calculating Q if there’s e.g: 2 reactants and e.g: 2O^2

A

[C][O2]^2
instead of times by 2, you square, if 3 lots you will cube

68
Q

METABOLISM
what reactions occur in stages 1-3 of glycolysis? what enzymes do this?

A

1) phosphorylation - HEXOKINASE
2) isomerisation - PHOSPHOGLUCOSE ISOMERASE
3) phosphorylation - PHOSPHOFRUCTOKINASE

69
Q

METABOLISM
what is the importance of glucose being isomerised to fructose in step 2?

A

2 G3P molecules can be created in step 5 , if didn’t happen 2 isomers (2 and 4c molecules would be created instead

70
Q

METABOLISM
summarise steps 1-5 of glycolysis

A

1) Glucose — glucose 6phosphate by HEXOKINASE, uses ATP

2) Glucose6phosphate — fructose6phosphate by PHOSPHOGLUCOSE ISOMERASE

3) fructose6phosphate — fructose1-6bisphosphate by PHOSPHOFRUCTOKINASE , uses ATP

4) fructose1-6bisphosphate — DHAP + 1XG3P by ADOLASE

5) DHAP — G3P so = 2xG3P instead

71
Q

what do kinases do?

A

add a phosphate, phosphorylated

72
Q

METABOLISM
Summarise stages 6-10 of glycolysis

A

6) 2xG3P — 2x1.3 bisphosphoglycerate by G3P DEHYDROGENASE , 2 NAD – 2 NADH (activated carrier molecule)

7) 2x1,3 bispho…. — 2x3phosphoglycerate by PHOSPHOGLYCERATE KINASE, 2 ADP –
2 ATP couple reaction with NAD-NADH prev

8) 2x 3 phosphoglycerate — 2x 2 phosphoglycerate by PHOSPHOGLYCEROMUTASE

9) 2x 2phosphoglycerate – 2x phosphoenolpyruvate by ENOLASE , loose 2H20

10) 2x phosphoenolpyruvate — 2xPyruvate by PYRUVATE KINASE , 2 ADP – 2ATP

73
Q

metabolism

what are the products of glycolysis?

A

net 2 ATP
2 NADH
2 pyruvate

74
Q

what is the rate limiting enzyme of glycolysis?
what is it activated and inhibited by?

A

PFK phosphofructokinase

activated by: AMP, F2,6 BP
inhibited by: ATP, as already high energy so don’t need more, low pH

75
Q
A

Sport Science sem 1 (3 decks)

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