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?

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?

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?

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?

25
Can proteins act as buffers?
Yes e.g. haemoglobin
26
What is primary structure?
the sequence of amino acid residues
27
What is secondary structure?
localised conformation of the polypeptide backbone
28
What is tertiary structure?
the three-dimensional structure of an entire polypeptide, including all its side chains
29
What is quaternary structure?
spatial arrangement of polypeptide chains in a protein with multiple subunits
30
What break alpha helixes?
proline residues
31
What component of bone and connective tissue is the most abundant protein in vertebrates?
collagen triple helix
32
What can lack of collagen cause?
bleeding gums, scurvy etc
33
Which are soluble in water, fibrous or globular proteins?
globular
34
What are examples of fibrous proteins?
keratin, collagen
35
Where do amino acids with hydrophobic side-chains tend to cluster?
centre of globular proteins
36
What change occurs in sickle cell anaemia?
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
Which proteins sometimes aid the folding process?
chaperones
38
What is prion disease an example of?
folding polypeptide disease
39
What does haemoglobin consist of?
four subunits two alpha and two beta chains each contains a haem group