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Principles Biochemistry > Introduction > Flashcards

Introduction Flashcards

1
Q

What is entropy?

A

disorder

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2
Q

Is free energy change positive or negative in exergonic reactions?

A

negative

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3
Q

In endergonic reactions, is total free energy of products more or less than in reactants?

A

more

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4
Q

Which type of reactions, exergonic or endergonic, can occur spontaneously?

A

exergonic

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5
Q

What happens to free energy released as you move closer to equilibrium?

A

increases

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6
Q

In readily reversible reactions (those close to equilibrium) what is the free energy change value?

A

close to zero

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7
Q

Which free energy change values are good in reactions which are control points?

A

large negative values

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8
Q

What type of free energy change value does conversion of ATP to ADP have?

A

large negative

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9
Q

Does the forward reaction of Glucose-6-phosphate into glucose-1-phosphate have a positive or negative value for free energy change?

A

positive

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10
Q

Is water polar or non polar?

A

polar

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11
Q

What are water molecules like?

A

bent, form a dipole, tetrahedral shape

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12
Q

What charge does hydrogen have?

A

partial positive charge

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13
Q

What shape are hydrogen bonds?

A

linear

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14
Q

In micelle formation what do the balls represent?

A

hydrophilic heads

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15
Q

In micelle formation what do the zag zag lines represent?

A

hydrophobic tails

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16
Q

What are the bonds between amino acids?

A

peptide

17
Q

From which terminal to which does the direction go in the peptide chain?

A

N terminal to C terminal

18
Q

What is the character and shape of peptide bonds?

A

partial double bond character
Peptide bonds are planar
Peptide bonds are strong and rigid
-important for folding of proteins

19
Q

Are acids proton donors or acceptors?

A

donors

20
Q

What is pH?

A

Measurement of the amount of protons in a solution

21
Q

What do amino acids without charged side groups exist as in neutral solution?

A

zwitterions with no net charge

22
Q

How many titratable groups do zwitterions have?

A

2

23
Q

What is the isoelectric pH?

A

The pH at which a molecule has no net charge

24
Q

Can the ends of proteins be ionised?

A

Yes

25
Q

Can proteins act as buffers?

A

Yes e.g. haemoglobin

26
Q

What is primary structure?

A

the sequence of amino acid residues

27
Q

What is secondary structure?

A

localised conformation of the polypeptide backbone

28
Q

What is tertiary structure?

A

the three-dimensional structure of an entire polypeptide, including all its side chains

29
Q

What is quaternary structure?

A

spatial arrangement of polypeptide chains in a protein with multiple subunits

30
Q

What break alpha helixes?

A

proline residues

31
Q

What component of bone and connective tissue is the most abundant protein in vertebrates?

A

collagen triple helix

32
Q

What can lack of collagen cause?

A

bleeding gums, scurvy etc

33
Q

Which are soluble in water, fibrous or globular proteins?

A

globular

34
Q

What are examples of fibrous proteins?

A

keratin, collagen

35
Q

Where do amino acids with hydrophobic side-chains tend to cluster?

A

centre of globular proteins

36
Q

What change occurs in sickle cell anaemia?

A

Single nucleotide sequence change
in coding region of the b chain of haemoglobin A
Results in altered protein
-valine in stead of glutamic acid

37
Q

Which proteins sometimes aid the folding process?

A

chaperones

38
Q

What is prion disease an example of?

A

folding polypeptide disease

39
Q

What does haemoglobin consist of?

A

four subunits
two alpha and two beta chains
each contains a haem group

Principles Biochemistry (4 decks)

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