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panic principles flashcards > biochemistry > Flashcards

biochemistry Flashcards

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
Q

what are the 3 types of secondary structures

A

alpha helix
beta strands and sheets
triple helix

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26
Q

where is the collagen triple helix found

A

bone and connective tissue

27
Q

how is a collagen triple helix formed

A

three helical chains twisted around each other to form a right handed superhelix

28
Q

what is the superhelix in the collagen triple helix called

A

tropocollagen

29
Q

what are the two types of tertiary structure

A

fibrous and globular proteins

30
Q

name two fibrous proteins

A

collagen and keratin

31
Q

name two globular proteins

A

myoglobin and haemoglobin

32
Q

what type of protein is water soluble

33
Q

what can denature a protein

A

heat
ph
a variety of chemicals

34
Q

what is a sugar and a base called

A

nucleoside

35
Q

what makes up a nucleotide

A

phosphate
sugar
base

36
Q

what end can new bases be added to in a growing DNA strand

37
Q

what enzyme adds new bases to a growing dna strand

A

DNA polymerase

38
Q

what bond forms between bases in dna strands

39
Q

what type of process is dna replication

A

semi conservative

40
Q

what is rrna

A

ribosomal rna - combines with protein to make ribosomes

41
Q

what is trna

A

transfer rna - carries the amino acids to be incorporated into the protein

42
Q

what is mrna

A

messenger rna- carries the genetic information for protein synthesis

43
Q

what determines what amino acid will bind to a specific trna

A

anticodon sequence

44
Q

how is transcription initiated

A

rna polymerase binds to promotors on DNA

45
Q

what enzyme separates dna strands

46
Q

what enzyme binds AA to their tRNA

A

aminoacyl-tRNA synthetases

47
Q

what enzyme catalyses formation of peptide bonds between amino acids

A

peptidyl transferase

48
Q

what moves the ribosome along mRNA

A

EF-2 (elongation factor)

49
Q

what is a point mutation

A

change in a single base in dna

50
Q

what is a missense mutation

A

change of amino acid sequence

51
Q

what is a nonsense mutation

A

creates a new termination codon, changes protein due to premature stop

52
Q

what is a silent mutation

A

degeneracy of genetic code, no effect on amino acid sequence or protein function

53
Q

what is a frameshift mutation

A

addition or deletion of 1 or 2 bases, changes triplets, amino acids and protein

54
Q

what is vmax

A

the maximum rate of a reaction

55
Q

what is the michaelis constant

A

Km - the substrate conc where the initial reaction rate is half vmax

56
Q

where is vmax on a graph

A

intersection of y axis

57
Q

where is km on a graph

A

intersection with x axis

58
Q

where does orthosteric inhibition occur

A

at the same site (competitive)

59
Q

what varies in competitive inhibition

60
Q

what varies in non competitive inhibition

61
Q

how is glucose transported

A

Na+/glucose symporters

GLUT 1-5 = passive facilitated diffusion transporters

62
Q

what is pyruvate and how many molecules are made during glycolysis

A

3 carbon molecules x2

63
Q

how many ATP produced in glycolysis

panic principles flashcards (7 decks)

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