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Neuroscience > Biochem > Flashcards

Biochem Flashcards

1
Q

Heat shock proteins as chaperones

A
  • Prevent aggregation of unfolded chain
  • Assist achieving proper protein conformation
  • Help transport partially folded proteins across membranes
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2
Q

Mislocalisation

A

process by which misfolded protein isn’t transported to its original location

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3
Q

formation of disulphide bonds between amino acids

A

Oxidation between cysteine residues

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4
Q

Which amino acid contains only 1 amino group?

A

Proline

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5
Q

TRUE/FALSE

Disulphide bonds are more common in intracellular proteins

A

FALSE

more common in extracellular, as they are less protected so need better support

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6
Q

Can peptide bonds rotate?

A

No - as they have double bond character due to resonance of e- between C and N

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7
Q

direction of residues in an alpha helix

A

hydrophobic residues point inward.

hydrophillic residues point outward.

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8
Q

β strands

A

polypeptide chains that are almost fully extended

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9
Q

β sheets

A

multiple β strands arranged side-side, stabilised by H bonds between C=O and N-H on adjacent strands

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10
Q

parallel β sheets

A

strands run in the same N- to C- terminal direction

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11
Q

antiparallel β sheets

A

strands run in opposite N- to C- terminal directions

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12
Q

screw sense

A

The direction in which a helical structure rotates with respect to its axis

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13
Q

native conformation

A

Polypeptide chain folds into a single stable shape, determined by sequence of amino acids & other important factors. Determines biological function

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14
Q

Helix-loop-helix

A

two helices connected by a turn

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15
Q

Coiled-coil

A

Two amphipathic α helices that interact in parallel through their hydrophobic edges

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16
Q

Helix bundle

A

Several α helices that associate in an antiparallel manner to form a bundle

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17
Q

β α β Unit

A

Two parallel β strands linked to an intervening α helix by two loops

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18
Q

Hairpin

A

Two adjacent antiparallel β strands connected by a β turn

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19
Q

β Meander

A

Antiparallel sheet composed of sequential β strands connected by loops or turns

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20
Q

Greek key

A

4 antiparallel strands (strands 1,2 in the middle, 3 and 4 on the outer edges)

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21
Q

β Sandwich

A

Stacked β strands or sheets

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22
Q

domain

A

Independently 3D folded, compact units in proteins

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23
Q

Proteins with very specific binding identities or catalytic functions are likely to possess

A

protein domains

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24
Q

All β

A

Only β sheets & connecting loop structures

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25
Q

α + β

A

Local clusters of α helices & β sheet in separate, clearly distinct regions

26
Q

Mixed α /β

A

Motifs such as the α β α unit, where regions of α helix and β strand alternate or are interdispersed

27
Q

All α

A

Consist almost entirely of α helices & connecting loops

28
Q

Categories of protein structure

A

All β
All α
Mixed α /β
α + β

29
Q

Aliphatic amino acids include

A 
glycine
alanine
valine
leucine
isoleucine
30
Q

Aromatic amino acids

A

phenylalanine
tyrosine
tryptophan
histidine

31
Q

sulfure containing amino acids

A

cysteine

methionine

32
Q

basic amino acids

A

lysine
histidine
arginine

33
Q

acidic amino acids

A

aspartate

glutamate

34
Q

amide versions of acidic amino acids

A

asparagine

glutamine

35
Q

alcohol amino acids

A

tyrosine
serine
threonine

36
Q

What is the most common structural motif in membrane proteins

A

spanning α-helices

37
Q

Valence shell

A

Outer electron shell

38
Q

Ligase

A

Enzyme which catalyses the joining of two substrates using ATP.

39
Q

Competitive inhibitor on kinetic constants

A

Bind to enzyme active site and raises Km value for enzyme

40
Q

Enzyme which cayalyses conversion of 2ADP to ATP and AMP

A

Adenylate Kinase

41
Q

How much free energy is released in ATP hydrolysis under normal physiological conditions?

A

Much more negative than ΔG°

42
Q

Which coenzyme is an oxidising agent used in catabolic reactions?

A

NAD+

43
Q

Which coenzyme is a reducing agent used in anabolic reactions?

A

NADPH

44
Q

First substance in glycolysis chain

A

GLucose

45
Q

Enzyme which converts glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate

A

GAPDH

46
Q

Enzyme which converts 1,3-bisphosphoglycerate to 3-phosphoglycerate

A

Phosphoglycerate kinase

47
Q

Enzyme involved in conversion of 3-phosphoglycerate to 2-phosphoglycerate during glycolysis

A

Phosphoglycerate mutase

48
Q

enzyme involved in conversion of 2-phosphoglycerate to Phosphoenolpyruvate during glycolysis

A

Enolase

49
Q

Enzyme which converts Phosphoenolpyruvate to pyruvate during glycolysis

A

Pyruvate kinase

50
Q

Other than glucose, what goes into glycolysis?

A

2 ADP + 2 NAD+ + 2 Pi

51
Q

Other than 2 pyruvate, what is produced during glycolysis

A

2 ATP

2 NADH

52
Q

Equation for anaerobic metabolism of pyruvate to form ethanol

A

Glucose (6C) + 2 ADP + 2 Pi + 2 H+ –> 2 Ethanol (2C) + 2 ATP + 2 CO2 + 2 H2O

53
Q

What enzyme converts pyruvate to lactate?

A

Lactate dehydrogenase

54
Q

what enzymes are involved in conversion of pyruvate to ethanol?

A

Pyruvate decarboxylase

Alcohol dehydrogenase

55
Q

Intermediate in alcoholic fermentation?

A

Acetaldehyde

56
Q

What regenerate NAD+ after use in lactic acid fermentation?

A

Glyceraldehyde 3-phosphate dehydrogenase in glycolysis

57
Q

Activators of PFK-1

A

AMP and Fructose-1,6-bisPhosphate

58
Q

Inhibitors of PFK-1

A

ATP and citrate

59
Q

The main regulatory step in glycolysis is that catalysed by:

A

Phosphofructokinase (step 3)

60
Q

Folding of polypeptide chain into secondary structure is accompanied by….

A

Negative free energy change

61
Q

What is the main driving force for protein folding?

A

Increase in entropy due to reorganization of associated water molecules

62
Q

During aerobic respiration, pyruvate from the glycolysis pathway enters the mitochondrial matrix via…

A

Co-transport with protons through a translocase

Neuroscience (22 decks)

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