Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Principles > Biochemistry > Flashcards

Biochemistry Flashcards

1
Q

Describe protons, electrons and neutrons in terms of :

  • charge
  • mass
A 
Protons - charge = +1
              - mass = +1
Electrons - charge -1
               - mass = 0
Neutrons - charge = 0
                - mass = +1
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Explain covalent bonding

A

sharing of electron pairs

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

Explain ionic bonding

A

attraction of opposite charges

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

Explain hydrophobic interactions

A

interaction of non polar substances in the presence of polar substances

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

Define electronegativity

A

the attractive force that an atomic nucleus experts on electrons within a bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Define REDOX

A
  • OILRIG
  • Oxidation - is loss of electrons
  • Reduction - is gain of electrons
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Final product of catabolism?

A

Carbon dioxide

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

Example of a monosaccharide

A

Glucose

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

Example of a disaccharide

A
  • sucrose

- lactose

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

Example of a polysaccharide

A

glycogen

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

Define thermodynamics

A

biophysical discipline which deals with the question if a process if energetically favourable

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

1st law of thermodynamics is….

A

energy is neither created nor destroyed

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

2nd law of thermodynamics is…

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
14
Q

Define entropy

A

free energy will tend towards an unusable state after multiple transformations
ΔS

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

What is enthalpy

A
  • heat constant

- ΔH

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

Equation for free energy

A

ΔG = ΔH – TΔS
T - is the temp in K

or

ΔG= (energy of the products)- (energy of the reactants)

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

ΔG= -ve

what does this imply?

A
  • exergonic reaction
  • energy of the products is less than that of the reactants
  • can occur spontaneously
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

ΔG= +ve

what does this imply?

A
  • endergonic reaction
  • energy of products is more than that of reactants
  • cannot occur spontaneously, requires the input of energy
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

What is the relationship between ΔG and equilibrium?

A

ΔG values near zero are characteristic of readily reversible reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

ADP is more stable than ATP: True/False

A

True

The negative charges close together in ATP put a strain on the molecule, making it less stable than ADP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Anhydride bonds are low energy:

True/False

A

False

Anhydride bonds are high energy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Define metabolism

A
  • all the reactions taking place in the body, divided into catabolism and anabolism
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Define Catabolism

A

breaking down complex molecules into smaller ones, releasing energy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Define 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
25
Q

There are always energy consuming steps in catabolic pathways.
True/ False

A

True

although catabolism releases energy, there are always energy consuming steps involved

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

Give an example of a catabolic pathway

A

Glycolysis

  • initial breakdown of glucose
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

Give an example of an anabolic pathway

A

Gluconeogenesis

  • making glucose from pyruvate
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

Reactions with large negative ΔG values are useful control points
True/False

A

True

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

What does hydrophilic mean?

A
  • water loving
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

What does hydrophobic mean?

A
  • water hating
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

What are hydrogen bonds?

A
  • covalent bonds
  • hydrogen bonded to a more electronegative atom
  • hydrogen gets a partially positive charge
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

Do hydrogen bonds tend to be _____

a) bent
b) linear

A
  • linear
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

What are amphipathic molecules?

A
  • have regions which are either hydrophobic or hydrophilic
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

What do amphipathic molecules form when in a polar substance?

A
  • micelles

hydrophilic heads in contact with water, hydrophobic tail towards the centre

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

What are the chemical groups that make up an amino acid?

A
  • amino group (NH2)
  • carboxyl (COOH)
  • hydrogen (H)
  • side chain (R)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

What is the alpha carbon?

A
  • the carbon bonded to the amino group, carboxyl, hydrogen and side chain
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

What does D & L mean in terms of amino acids?

A
  • Sterochemistry
  • D & L are stereoisomers

( cannot be superimposed on each other)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

What makes amino acids acidic?

A
  • additional COOH group
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

What is a useful property of acidic buffers?

A
  • can be used as buffers
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

What is a useful property of basic buffers?

A
  • used as buffers
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

How can you identify a basic buffer?

A
  • long hydrocarbon chain
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

What are the 4 elements that make up a peptide bond?

A
  • carbon
  • oxygen
  • nitrogen
  • hydrogen
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

What does it mean “peptides have direction”

A
  • depending on the end terminal will say if it is N or C terminal
  • N terminal - amino group
  • C terminal - Carboxyl group
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q

In which direction is a peptide chain?

A
  • N –> C
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
Q

Peptide bonds are _____ in shape
a) planar
b ) 3 dimensional

A
  • a

- peptide bonds are planar

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q

Peptide bonds are ____

a) strong
b) weak

A
  • a

strong and rigid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

Acids are proton ____

A

donators

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

Bases are proton ____

A

acceptors

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
49
Q

What is the strength of an acid based on?

A
  • how readily it donates a proton to a base
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
50
Q

What is the equation for the acid dissociation?

A

Ka = [H+][A-]
—————
[HA]

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
51
Q

pH is equal to—-

A

pH = -log10 [H+]

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
52
Q

What is a buffer?

A
  • a solution to control the pH of a reaction
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
53
Q

Name of an amino acid that exists without charged groups?

A
  • zwitterions
  • no net charge
  • contains 2 tritatable groups
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
54
Q

name given to the pH where a molecule has no net charge?

A
  • isoelectric pH
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
55
Q

What is the primary structure of a protein?

A
  • sequence of amino acids
56
Q

what is the secondary structure of a protein?

A
  • localised confirmation of the polypeptide backbone
57
Q

what is the tertiary structure of a protein?

A
  • 3d shape
58
Q

What is the quaternary structure of a protein?

A
  • the spatial arrangement of polypeptide chains with multiple subunits
59
Q

where can a polypeptide rotate?

A
  • between:
  • a carbon and amino group
  • a carbon and carboxyl group
60
Q

3 types of secondary structures?

A
  • a helix
  • b sheet
  • triple helix
61
Q

Explain a helix?

A
  • secondary structure
  • 1 rod like chain
  • right handed
62
Q

explain beta sheets?

A
  • secondary structure
  • may be parallel or antiparallel
  • may contain turns
63
Q

explain triple helix?

A
  • secondary structure

- 3 left handed rods

64
Q

example of a triple helix protein?

A
  • collagen
65
Q

2 types of tertiary structures?

A
  • fibrous (paralel along single axis)

- globular (folded spherical)

66
Q

tertiary protein interactions?

A
  • covalent disulphide bonds
  • hydrogen bonds
  • hydrophobic interactions
  • salt bridges
67
Q

“polar groups are more likely to be in the inside of a polypetide”

true or false?

A
  • false

- more likely to be on outside for interactions with water

68
Q

explain myoglobin

A
  • globular protein
  • haem group
  • stores oxygen in muscle
69
Q

explain haemoglobin

A
  • globular protein
  • 4 subunits
  • 2 alpha + 2 beta chains
  • transports oxygen in blood
70
Q

what is the name of the molecule which helps protein folding?

A
  • chaperones
71
Q

What is a nucleoside?

A
  • base + sugar
72
Q

What is a nucleotide?

A
  • nucleoside + phosphate group(s)
73
Q

What end are nucleotides added to?

A
  • 3’ end
74
Q

DNA is a continuous process

true or false?

A
  • false

- discontinous

75
Q

What are okazaki fragments

A
  • formed from the laggin strand
76
Q

what in built mechanism does DNA have to pick up errors?

A
  • exonuclease activity
  • 3’ –> 5’ direction
  • removes incorrect nucleotides
77
Q

3 types of RNA?

A
  • tRNA
  • mRNA
  • rRNA
78
Q

What is tRNA

A
  • carries amino acids to be incorportated in a protein
79
Q

What is mRNA

A
  • carries genetic information for protein synthesis
80
Q

What is rRNA

A
  • combines with a protein to form a ribosome
81
Q

What is a TBP?

A
  • TATA Box Binding Protein
  • recognises TATA boc
  • part of TFIID
82
Q

Name a transcription factor?

A

TFIID

83
Q

What are introns

A
  • non coding regions

- must be spliced

84
Q

In relation to amino acids what does degenerate mean?

A
  • many amino acids have more than one codon
85
Q

In relation to amino acids what does unambiguous mean?

A
  • each codon only codes for 1 amino acid
86
Q

What protein binds amino acids to corrosponding tRNA/

A
  • aminoacyl-tRNA sythatase
87
Q

What are the names of the 3 binding sites in a ribosome?

A
  • A (amioacyl)
  • P (peptidyl)
  • E (Exit)
88
Q

An example of a start codon

A

AUG

89
Q

Nonsense mutation?

A
  • creates a premature stop codon
90
Q

Missense mutation?

A

amino acid sequence changed

91
Q

Free ribosomes make proteins for where?

A
  • nucleus
  • cytosol
  • mitochondria
92
Q

Bound ribosomes make proteins for where?

A
  • plamsa membrane
  • golgi apparatus
  • ER
93
Q

What are enzymes?

A
  • catalyse chemical reactions
  • speeds up a reaction without altering the equilibrium
  • provide an alternative pathway
94
Q

What is a cofactor and name an example?

A
  • required for the action of an enzyme
  • inorganic –> metals
  • zinc, iron, copper
95
Q

What is a coenzymes and name an example

A
  • required for the action of an enzyme
  • organic —> vitamins
  • NAD+
96
Q

What is an isozyme?

A
  • isoform of an enzyme, catalyse the same reaction but have different properties/structure
97
Q

What is a zymogen?

A
  • inactive precursors of an enzyme

- needs to be cleaved to become active

98
Q

Describe what enzyme behavior would look like on a Michaelis Menten model?

A
  • hyperbolic in shape
  • Vmax and Km values
  • Sustrate on x axis
  • rate on Y axis
99
Q

What is Vmax?

A
  • infinite substrate will approach a maximal rate
100
Q

What is Km?

A
  • the concentration of substrate required to produce a half maximal effect
101
Q

How can Km be calculated?

A

Km= k-1+k2/k1

102
Q

Why is a lineweaver plot better than michaelis menten model for determining Km and Vmax?

A
  • kinetics is never linear, will never reach exact Vmax on michaelis menten
103
Q

Where is 1/Vmax seen on lineweaver plot?

A
  • Y axis
104
Q

Where is -1/Km seen on lineweaver plot?

A
  • X axis
105
Q

What effect does a competitive inhibitor have on a lineweaver plot?

A
  • Vmax remains the same

- Km is increased

106
Q

What effect does a non-competivite inhibitor have on a lineweaver plot?

A
  • Vmax is reduced

- Km remains the same

107
Q

Explain feedback inhibition

A
  • the end product of a reaction may inhibit one of the beginning rate limiting enzymes
  • prevents a build up of intermediates that may be harmful
  • allosteric control
108
Q

What is different about allosteric enzymes in terms of the Michaelis Menten model?

A
  • do not follow a hyperbolic graph
  • instead they are sigmoidal
  • show co-operativity
109
Q

What can be used to control allosteric enzymes?

A
  • activators

- inhibitors

110
Q

Define metabolism

A
  • all chemical reactions that maintain the living state of cells and organisms
111
Q

Define anabolism?

A
  • assimilation of molecules from building blocks of life

- requires energy

112
Q

Define catabolism?

A
  • breakdown of molecules to obtain building blocks

- energy yielding

113
Q

Name a monosccharide

A
  • glucose
114
Q

Name a disaccharide

A
  • lactose
115
Q

Name a polysaccharide

A
  • glycogen
116
Q

How does glucose get transported from cells?

A
  • GLUT receptors

- conformational changes allowing binding at one side and then release at the other

117
Q

Define glycolysis

A
  • the initial pathway which is involved in the conversion of glucose to 2 pyruvate
118
Q

Explain the intermediates of glycolysis?

A
  • glucose
  • fructose-1,6-bisphosphate
  • 2 triose phosphate
  • 2 pyruvate
119
Q

What are the names of the 3 enzymes that control glycolysis?

A
  • hexokinase (controls subsrate entry)
  • phosphofructokinase (rate flow control)
  • pyruvate kinase (end product formation)
120
Q

What is the name given to the ATP/AMP ratio?

A
  • energy charge
121
Q

In the environment of not enough oxygen what occurs?

A
  • mitochondrial metabolism inhibited
  • NADH ferments pyruvate –> lactic acid
  • NADH regenerated
122
Q

How is NAD+ regenerated?

A
  • oxidative metabolism of pyruvate
123
Q

Where does the TCA occur?

A
  • mitochondria
124
Q

How does pyruvate enter the mitochondrial matrix?

A
  • H+ gradient

- pyruvate transporters

125
Q

what catalyses pyruvate to acetyl CoA?

A
  • Pyruvate dehydrogenase complex
126
Q

What can the reaction from pyruvate to acetyl CoA be called?

A
  • oxidative decarboxylation
127
Q

Where are enzymes for the TCA located?

A
  • mitochondrial matrix

- except succinate dehydrogenase (inner mitochondrial membrane)

128
Q

Electrons from NADH and FADH2 are used to reduce ___ to ____

A
  • electrons are used to reduce O2 to H20
129
Q

The energy of NADH and FADH2 is used to ____

A
  • pump protons from mitochondrial matrix
130
Q

What are the names of the 2 transporters of NADH and FADH2?

A
  • Glycerol-3-phosphate

- malate-aspartate

131
Q

How is phosphoryl tranfer potential measured?

A
  • measured by the free energy change for hydrolysis of ATP
132
Q

How is electron transfer potential measure?

A
  • measured by the redox potential of a compound
133
Q

NADH enter what complex?

A
  • complex I
134
Q

FADH2 enter what complex?

A
  • complex II
135
Q

Final electron acceptor in the electron transport chain?

A
  • O2
136
Q

1 Glucose molecule can make how many ATP molecules?

A
  • 30-32 ATP molecules

Principles (11 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions