biochemistry Flashcards

(63 cards)

1
Q

how is a covalent bond formed

A

when unpaired electrons are shared

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2
Q

what is a redox reaction

A

electrons transferred from one molecule to another

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3
Q

what is oxidation

A

loss of electrons

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4
Q

what is reduction

A

gain of electrons

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5
Q

what is an exergonic reaction

A

delta g negative

occur spontaneously

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6
Q

what is an endergonic reaction

A

delta g positive

cant occur spontaneously

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7
Q

what is coupled to allow many reactions in the body to occur

A

an unfavourable reaction (positive delta G) and a favourable one (negative delta G) such as breakdown of ATP and H2O

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8
Q

what is metabolism

A

all the reactions taking place in the body

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9
Q

what can metabolism be divided into

A

catabolism and anabolism

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10
Q

what is catabolism

A

breadking down complex molecules into smaller ones

releases energy

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11
Q

what is anabolism

A

synthesising complex molecules from smaller ones

consumes energy

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12
Q

what is an acid

A

proton donaters

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13
Q

what is a base

A

proton acceptors

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14
Q

what does the strength of an acid depend on

A

how readily it donates a proton

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15
Q

how is acid strength measured

A

the acid dissociation constant, Ka

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16
Q

what is the equation for pH

A

pH = -log10[H+]

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17
Q

what is the Henderson-Hasselbalch equation

A

ph = pka + log [base]/[acid]

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18
Q

what is a buffer

A

a solution used to control the ph of a reaction mixture

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19
Q

when does ph = pka

A

when the [acid] is equal to the [conjugate base]

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20
Q

what is the primary structure

A

one dimensional, the sequence of amino acid residues

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21
Q

what is the secondary structure

A

the localised conformation of the polypeptide backbone

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22
Q

what is the tertiary structure

A

the 3D structure of an entire polypeptide

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23
Q

what is the quaternary structure

A

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

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24
Q

what bond holds secondary structures together

A

hydrogen

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25
what are the 3 types of secondary structures
alpha helix beta strands and sheets triple helix
26
where is the collagen triple helix found
bone and connective tissue
27
how is a collagen triple helix formed
three helical chains twisted around each other to form a right handed superhelix
28
what is the superhelix in the collagen triple helix called
tropocollagen
29
what are the two types of tertiary structure
fibrous and globular proteins
30
name two fibrous proteins
collagen and keratin
31
name two globular proteins
myoglobin and haemoglobin
32
what type of protein is water soluble
globular
33
what can denature a protein
heat ph a variety of chemicals
34
what is a sugar and a base called
nucleoside
35
what makes up a nucleotide
phosphate sugar base
36
what end can new bases be added to in a growing DNA strand
3 prime
37
what enzyme adds new bases to a growing dna strand
DNA polymerase
38
what bond forms between bases in dna strands
hydrogen
39
what type of process is dna replication
semi conservative
40
what is rrna
ribosomal rna - combines with protein to make ribosomes
41
what is trna
transfer rna - carries the amino acids to be incorporated into the protein
42
what is mrna
messenger rna- carries the genetic information for protein synthesis
43
what determines what amino acid will bind to a specific trna
anticodon sequence
44
how is transcription initiated
rna polymerase binds to promotors on DNA
45
what enzyme separates dna strands
helicase
46
what enzyme binds AA to their tRNA
aminoacyl-tRNA synthetases
47
what enzyme catalyses formation of peptide bonds between amino acids
peptidyl transferase
48
what moves the ribosome along mRNA
EF-2 (elongation factor)
49
what is a point mutation
change in a single base in dna
50
what is a missense mutation
change of amino acid sequence
51
what is a nonsense mutation
creates a new termination codon, changes protein due to premature stop
52
what is a silent mutation
degeneracy of genetic code, no effect on amino acid sequence or protein function
53
what is a frameshift mutation
addition or deletion of 1 or 2 bases, changes triplets, amino acids and protein
54
what is vmax
the maximum rate of a reaction
55
what is the michaelis constant
Km - the substrate conc where the initial reaction rate is half vmax
56
where is vmax on a graph
intersection of y axis
57
where is km on a graph
intersection with x axis
58
where does orthosteric inhibition occur
at the same site (competitive)
59
what varies in competitive inhibition
Km
60
what varies in non competitive inhibition
Vmax
61
how is glucose transported
Na+/glucose symporters | GLUT 1-5 = passive facilitated diffusion transporters
62
what is pyruvate and how many molecules are made during glycolysis
3 carbon molecules x2
63
how many ATP produced in glycolysis
4