Biochem Flashcards

(30 cards)

1
Q

What kind of bonding is shown in the phospholipid bilayer

A

Hydrophobic forces between long hydrophobic chains in midlayer

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2
Q

What is acylation

A

Addition of a group containing a carbon double bonded to oxidation

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3
Q

What type of reaction is condensation

A

Anabolic (2 smaller molecules are ‘built up’ to a larger molecule)

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4
Q

What type of reaction is hydrolysis

A

Catabolic (larger molecule broken down)

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5
Q

What is the final oxidative stage of carbon

A

Carbon dioxide

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6
Q

What is metabolism

A

Net oxidative process where carbon is fully reduced to an oxidised state

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7
Q

Functions of biomolecules

A

Information storage
Structural
Energy generation
Energy/currency storage - atp
Communication - receptors, hormones etc

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8
Q

What are the classes of biomolecules

A

Peptides and proteins
Lipids
Nucleic acids
Carbohydrates - saccharides

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9
Q

How is energy stored within the cell

A

Through carbohydrates in the form of carbon chains

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10
Q

What makes the glucose molecules a reducible target

A

The oxygen atom between carbon 1 and carbon 5

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11
Q

How are disaccharides formed

A

Covalent bonds between c1 - c4 or c1-c2

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12
Q

What is polymeric glucose

A

Glycogen - energy store

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13
Q

Which carbon links form the polymer, glycogen?

A

C1-c6

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14
Q

When is some energy unavailable to do work

A

When energy is transformed

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15
Q

What is an exergonic reaction

A

If the free energy change is negative

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16
Q

When can reactions occur spontaneously

A

If the change in free energy is negative

17
Q

What are examples of exergonic reactions

A

Energy left over from reaction can do work such as conversion of glycogen to glucose

18
Q

What are endergonic reactions

A

Free energy change is positive
Cannot occur spontaneously - need an input of energy

19
Q

What shape is a water molecule

A

Tetrahedral (lone pairs)

20
Q

What substances are hydrophilic

A

Ionic and polar (can dissolve in water)

21
Q

What is the isoelectric point of a molecule

A

The pH at which a molecule has no net charge

22
Q

How many pKa values do amino acids with no charge have

A

2 as they have 2 titratable groups

23
Q

How can proteins act as buffers

A

Several amino acid side chains can be ionised

24
Q

What happens to a protein if there is a change in pH

A

Can change ionisation of a protein which can lead to a change in structure therefore function

25
How is hydrogen bonding promoted in biomolecules
Difference of EN of atoms in water create dipoles
26
How can amphipathic molecules span polar and non-polar environments
Due to hydrophobic and hydrophilic domains
27
Where do the unique buffering abilities of protein come from
Zwitterionic properties of amino acids
28
How can changes in protein conformation arise
Redox interaction that affect the state of metal ion centres Disulphide bridges Salt bridging Hydrophobic interactions Electrostatic (polar?) interactions
29
What strutcure of the protein is important to its function
Tertiary (peptide fold)
30
What can changes in amino acid sequence lead to
Altering of function