Biochemistry Flashcards

1
Q

What is the first law of thermodynamics?

A

Energy is neither created nor destroyed, it can only be transferred from one form to another

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What is the second law of thermodynamics

A

When energy is converted from one form to another, some of that energy becomes unavailable to do work

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What are the building blocks of carbohydrates?

A

monosaccharides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What is the difference between monosaccharides, disaccharides and polysaccharides?

A

mono- carbohydrates with single ring structure

di- double ring structure

poly- long chains of monosaccharides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

what are the 4 major classes of biomolecules

A
  • peptides and proteins
  • lipids
  • nucleic acids
    -carbohydrates
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What are the meanings of entropy and enthalpy

A

entropy- disorder
enthalpy- heat content

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

what is an exergonic reaction?

A

total free energy of products is less than total free energy of the reactants- reactions can occur spontaneously.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What is an endergonic reaction?

A

total free energy of the products is more than the total free energy of the reactants - cannot occur spontaneously

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What do endergonic reactions require in order to proceed?

A

An input of energy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

How is the free energy related to equilibrium?

A

Reversibility of the reaction increases the closer the free energy is to zero.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

In what way can endergonic reactions be allowed to proceed

A

When this unfavourable reaction is coupled to a favourable exergonic reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What does metabolism mean?

A

All of the chemical reactions taking place within the body

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What is meant by catabolism?

A

Breaking down complex molecules into smaller ones and releasing energy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Are catabolic reactions exergonic or endergonic

A

exergonic reactions- energy yielding

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

what is meant by anabolism

A

Synthesising complex molecules out of smaller ones in energy consuming reactions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Are anabolic reactions exergonic or endergonic

A

endergonic reactions - require energy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What is a polar molecule?

A

A molecule in which electrons are shared unequally due to a difference in electronegativity, this causes a difference in charge from one side of the molecule to the other.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

What shape do water molecules have and how are they held together?

A

They have a tetrahedral shape and they are held together with hydrogen bonds

19
Q

What is a hydrogen bond?

A

A covalent bond between hydrogen and a more electronegative atom that creates a polarised bond

20
Q

Are hydrogen bonds reversible or irreversible?

A

They are reversible and allow reversible change in biomolecules

21
Q

What is an amphipathic molecule?

A

Molecules which are both hydrophilic and hydrophobic, they have a polar head at one end and a non polar tail at the other end

22
Q

What is the common structure of all amino acids?

A

an alpha carbon bonded to
- an amine group
- a carboxyl group
- a hydrogen
- an R group

23
Q

what are the 4 classifications of amino acids?

A
  • hydrophobic
  • polar
  • acidic
  • basic
24
Q

What is a peptide bond?

A

The bond that links amino acids.

25
Q

What are peptide bonds important for?

A

They are important for the folding of proteins

26
Q

What are the two ends of a peptide called

A

The start is called the N - terminal residue and the end is called the C- terminal residue

27
Q

Is a base a proton donor or acceptor?

A

Proton acceptor

28
Q

Is an acid a proton acceptor or donor?

A

Proton donor

29
Q

What does the strength of an acid depend on?

A

How readily it donates a proton to a base

30
Q

What is the PH a measure of?

A

Measurement of the amount of protons in a solution

31
Q

How do you calculate the PH of a substance?

A

PH= -log10[H+]

32
Q

What is the purpose of the Henderson Hasselbach equation?

A

connects the Ka of a weak acid with the PH of a solution containing this acid

33
Q

What is the Henderson- Hasselbalch equation?

A

pH=pKa+ log[A]/[HA]

34
Q

What is the purpose of a buffer solution?

A

To control the PH of a reaction mixture -

35
Q

How does changing PH affect a protein?

A

It can change the ionisation of the protein therefore changing its structure and function

36
Q

What is the primary structure of a protein?

A

The sequence of the amino acids in the polypeptide

37
Q

What is the secondary structure of a protein?

A

Localised conformation of the polypeptide backbone

38
Q

What are the three types of secondary structure?

A

Alpha helix, beta pleated sheets and triple helix

39
Q

What type of bonding is involved in the secondary structure of proteins?

A

Hydrogen Bonding

40
Q

What is the tertiary structure?

A

The 3D structure of an entire polypeptide

41
Q

What are the two types of tertiary structures?

A

Fibrous proteins - e.g collagen (insoluble in water)

Globular proteins- spherical (haeoglobin) - soluble in water

42
Q

What is the quaternary structure?

A

The spatial arrangement of polypeptide chains in a protein with multiple subunits

43
Q

example of a protein with a quaternary structure?

A

Haemoglobin

44
Q
A