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Biochemistry Flashcards

(115 cards)

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1
Q

condensation

A

water removed

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2
Q

hydrolysis

A

water added

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3
Q

Oxidation

A

loss of electrons

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4
Q

reduction

A

gain of electrons

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5
Q

protein

A

chain of amino acid

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6
Q

peptide

A

chains of amino acids smaller than protein

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7
Q

lipids

A

fatty acids
soluble in inorganic substances but insouble in water
eg cholesterol

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8
Q

nucleic acid

A

composed of nucleotides

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9
Q

carbohydrates

A

composed of carbon, hydrogen and oxygen

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10
Q

efficiency of converting energy

A

energy cannot be created, only change form
converting energy from one source to another is not 100% efficient,and each time it occurs some of the energy becomes unusable
e.g. eventually there will be no usable energy

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11
Q

enthalpy

A

heat H

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12
Q

entropy

A

disorder S

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13
Q

change in free energy

A

ΔG° = ΔH° - TΔS°
temp in kelvin

ΔG° = energy of the products- energy of the reactants

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14
Q

free energy

A

the internal energy of a system minus the amount of energy that cannot be used to perform work.

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15
Q

exergonic reactions

A

ΔG° = -ve
the energy of the products is less than the energy of the reactants
can occur spontaneously

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16
Q

endergonic reactions

A

ΔG° = +ve
energy of the products is higher than the energy of the reactants
cannot occur spontaneously

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17
Q

what drives endergonic reactions

A

coupling to a exergonic reaction
many reactions coupled to ATP
ATP is highly unstable so produces energy by breaking 1 phosphate bond, stored as ADP

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18
Q

metabolism

A

all anabolic and catabolic reactions

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19
Q

catabolism

A

breaking down larger molecules to produce smaller ones
there are some energy consuming stages but net gain
exergonic and oxidative

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20
Q

anabolism

A

producing larger molecules from smaller molecules requiring ATP
endergonic and reductive

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21
Q

what is the ΔG of control reactions

A

large -ve ΔG° as the reaction will be mostly irreverisble as would require so much energy

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22
Q

water

A

polar, forms a dipole, ionic substances dissolve in water

non-polar substances are insoluble in water

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23
Q

amphiphilic

A

polar and non-polar

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24
Q

hydrophobic

A

water hating

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25
hydrophilic
water loving
26
amino acids
form proteins NH2, COO, H and side chain amino group, carboxyl and H
27
categories of amino acid
acidic, basic, polar and non-polar
28
direction of amino acids
N terminus (amino group) to the C terminus (carboxyl terminus)
29
strength of peptides bond and the importance
strong, important for folding
30
acids
donate a proton( H+) strength of an acid depends on how readily it donates the H+ e.g. strong acids will readily donate the H+ in water and fully ionise
31
Bases
Proton acceptors
32
pH
the concentration of H+ ions
33
buffer
solution to control the pH of a reaction mixture | resist pH change
34
proteins as buffers
proteins contain amino acid groups and carboxyl groups so are able to act as buffer a change in pH can cause ionisation of proteins resulting in a change in protein structure and function
35
primary protein
sequence of amino acids
36
secondary protein
polypeptide backbone
37
tertiary protein
3D structure
38
quaternary protein
spatial arrangement of polypeptide chains with multiple subunits
39
Polypeptide rotation
polypeptides can rotate around the alpha carbon and the carboxyl group and they can rotate around the alpha carbon and the amino group.
40
bonds in secondary proteins
hydrogen bonds
41
3 types of secondary structure
1) alpha helix 2) beta pleated sheat 3) collagen triple helix
42
alpha helix
the H in the NH2 forms a bond with the O from C
43
B pleated sheet
zig zag
44
parallel B sheet
both strands start and end same place | e.g. both N-C or both C-N
45
antiparallel B sheet
the strands start and finish in different places eg one is C-N and the other is N-C
46
collagen triple helix
component of bone and connective tissue
47
bonds in primary protein structure
peptide
48
tertiary proteins
fibrous and globular proteins
49
bonds stabilising tertiary structure
ionic bonds hydrophobic bonds convalent disulphide bonds hydrogen
50
quaternary
proteins with more than 1 polypeptide chain
51
transcription
RNA polymerase is used to transfer DNA to RNA
52
translation
ribosomes translate the mRNA/RNA to an amino acid sequence
53
nucleoside
base and sugar
54
nucleotide
nucleoside and phosphate
55
bonds between bases
AT is a double bond | CG is a triple bond
56
DNA polymerase
synthesise DNA from deoxyribonucleotides | enzyme for DNA replication
57
3'
has a free phosphate
58
5'
has a free deoxyribose
59
differences between DNA and RNA
RNA is single stranded while DNA is double stranded. RNA has a sugar called ribose while DNA has a sugar called deoxyribose. RNA has the base uracil while DNA has the base thymine.
60
Replication
many sites of origin of DNA replication nucleotides can only be added to the 3' end leading strand is continuous lagging strand is added in short segments and joineed together by DNA ligase
61
DNA ligase
joins together the okazaki fragments of the lagging strand
62
chromosomes
carry DNA one from mum and one from dad 23 pairs of chromosomes in each human cells
63
rRNA
ribosomal ribonucleic acid | combines with proteins to form ribosomes where protein synthesis takes place
64
types of rna
ribosonal rna messenger RNA transfer RNA
65
mRNA
transfers a copy of the genetic code from the nucleus to ribosomes for protein synthesis
66
tRNA
translates nucleotides to amino acids
67
steps of transcription
``` RNA polymerase binds DNA sequence separates Transcription is initiated Elongation: addition of further nucleotides Termination: release of finished RNA ```
68
Types of mutation
``` silent missense nonsense chromosomal frameshift point ```
69
point mutation
change in a single base
70
missense mutation
change in amino acid sequence and can change proteins function
71
nonsense mutation
creates anew termination codon
72
silent mutation
no chance on amino acid sequence
73
frameshift mutation
insertion or deletion
74
chromosomal mutation
large sections of the genome affected
75
what happens to the finished protein
Tareted to location modified unwanted proteins are degraded
76
factors
initiation, termination and elongation all require factors
77
post translational modifications
glycosylation disulphide bonds cleavage
78
Enzymes affect on equilibrum position
do not affect the equillibrum of reactions
79
specificity
enzymes are v specific and stabilise the transition state
80
how do enzymes reduce the actiation energy
provide an alternative pathway
81
cofactors
assist enzymes | metal ions
82
coenzymes
aid enzymes | organic molecules
83
prosthetic group
tightly bought coenzymes
84
haloenzymes
enzymes with cofactor
85
apoenzyme
enzyme without cofactor
86
isoenzymes
catalyse same reaction but different properties and structure
87
phosphorylation
can activate or deactivate a protein
88
irreversible convalent modifiation
activate of enzymes | eg digestive enzymes
89
Vmax
Maximum velocity of a reaction ie inifinite substrate | the reaction velocity never reaches V max
90
Km
substrate concentration that gives half of V max
91
orthosteric inhibition
inhibitor binds at active site and blocks substrate acess
92
allosteric inhibition
inhibitor binds at a site other than the active site and changes conformation
93
irreversible inhibition
non-competitive, cannot be reversed, usually involves the formation or breakage of a convalent bond
94
competitive inhibition on graph
Km varies but Vmax does not change
95
non-competitive inhibition on graph
Km stays the same but Vmax changes
96
allosteric enzymes
contain multiple subunits. binding of a substrate to one subunit causes a conformational change which causes a conformational change in the other subunits increasing their affinity for the substrate
97
increasing substrate conc in allosteric enzymes
sigmoid curve
98
what does a sigmoid curve show
cooperative behaviour
99
what controls allosteric enzymes
allosteric inhibitors and allosteric activators
100
glucose fermented
lactate
101
glucose oxidised
pyruvate | ribose
102
glucose stored
glycogen
103
glucose transporters
``` GLUT1: brain GLUT2: liver GLUT3:brain GLUT4: muscles GLUT5: gut ```
104
where does glycolysis take place?
cyptoplasm
105
hexokinase
regulates how much glucose is converted to glucose pyruvate
106
phosphofructokinase
rate of flow
107
pyruvate kinase
how much pyruvate leaves
108
names of the control enzymes in glycolysis
hexokinase phosphofructokinase pyruvate kinase
109
glycolysis activators
amp | fructose-2,6- biphosphate
110
glycolysis inhibitors
ATP, citrate and H+
111
where does the citric acid cycle take place
mitochondria
112
orthosteric enzymes
bind to the active site
113
isoenzymes
same function different structure
114
kinases
phosphorylate
115
zymogens
an inactive substance which is converted into an enzyme when activated by another enzyme

Principles (6 decks)

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