biomolecules Flashcards

(86 cards)

1
Q

what are the 4 primary metabolites ?

A

proteins, nucleic acids, carbohydrates and lipids
(living things need all four of these)

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2
Q

nucleic acids are biopolymers with … as the monomer and di,tri, oligo-nucleotides in between

A

nucleotides

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3
Q

proteins are biopolymers with … … as the monomers and di, tri, oligopeptides in between

A

amino acids

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4
Q

lipids are not polymers but contain 1-3 … …, usually attached to …

A

fatty acids
glycerol

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5
Q

all the chemical reactions that make up life take place in … as a solvent

A

water

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6
Q

atoms within molecules are held together by … …

A

covalent bonds

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7
Q

molecules attract each other with weaker interactions such as :

A

hydrogen bonds
electrostatic forces
hydrophobic interactions

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8
Q
A
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9
Q

describe h-bonding

A

occurs when a hydrogen attached to an electronegative element is attracted to an atom with an available lone pair

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10
Q

explain what electrostatic interactions are.

A

when positively charged and negatively charged species attract one another

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11
Q

explain hydrophobic interactions.

A

hydrophobic/lipophilic molecules will attract one another when placed in water.

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12
Q

why do hydrophobic molecules attract one another when placed in water ?

A

because they break up the h-bonding network in water (this is destabilising for the system), so by clumping together, the hydrophobic molecules reduce the overall damage to the h-bonding network

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13
Q

the entire collection of genes is called the …

A

genome

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14
Q

the genome is kept in …

A

the nucleus of eukaryotes in a number of chromosomes

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15
Q

a chromosome is a …

A

molecule of dna

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16
Q

a gene is a stretch of dna which…

A

codes for a protein

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17
Q

dna carries the … … … which effectively makes it an instruction book for creating an organism

A

code for proteins

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18
Q

the dna code is … onto mrna which is another nucleic acid and this leaves the nucleus

A

transcribed

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19
Q

when the dna code in on a molecule of rna, it is … to a new protein

A

translated

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20
Q

how is a double helix formed ?

A

two strands of the polymer which are held together by hydrogen bonds.

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21
Q

what is the polymer backbone made out of ?

A

is made up of sugar and phosphate

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22
Q

inside the helix are the …

A

bases

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23
Q

what do bases do ?

A

they carry the code for proteins and allow replication and transcription

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24
Q

can faulty dna be passsed on through generations ?

A

yes

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25
how can dna be damaged ?
can be damaged during life, either by mistakes in copying, or damage by outside causes
26
if dna is damaged then the gene product (protein) will be ...
missing or malfunctioning. this can lead to ill effects
27
is dna damaged and copied badly all the time ?
yes
28
is there a system of dna repair in place in human cells
yes and it deals with most problems
29
what would happen if the system of dna repair in human cells fails ?
there are tumour-supressor systems and apoptosis to remove mutated cells without cancer happening
30
proteins are polymers of ... ...
amino acids
31
how many levels of structure do proteins have ?
4 primary, secondary, tertiary and quaternary
32
what are the two types of protein ?
structural and functional
33
what are some examples of functional proteins ?
enzymes, hormones/growth factors, antibodies, factors involved in blood coagulation, receptors and ion channels
34
what is the definition of primary structure ?
the amino acid sequence
35
what is the definition of secondary structure ?
local 3d structure
36
what is the definition of tertiary structure ?
global 3d structure
37
what is the definition of quaternary structure ?
association of multiple polypeptides
38
side chains can be ...
glycine hydrophobic h-bonding charged
39
what does it mean if a side chain of an amino acid is glycine ?
this means there is no side chain and hydrophilic
40
what does it mean if the amino acids side chain is hydrophobic ?
a hydrophobic side chain would mean that it is greasy and lipophilic
41
what does it mean if an amino acid side chain has h-bonding ?
a side chain that has h-bonding would be more polar and hydrophilic
42
what does it mean if an amino acids side chain is charged ?
this means it is either negative, positive or polar and hydrophilic
43
what structures do secondary structure proteins form when regular ?
alpha helix and beta sheets
44
what structures do secondary structure proteins form when irregular ?
turns, loops, coils etc.
45
describe in detail what tertiary structure is .
the helices, sheets and loops of a protein can be combined in many ways to give a global 3d structure
46
tertiary structure is ...
vital to function
47
what is denaturation ?
this is when a functional protein changes its tertiary and quaternary structure
48
how do proteins become denatured ?
denaturation can happen through chemical reactions, heat, ph or changes in solvent
49
what is the function of an enzyme ?
enzymes catalyse reactions
50
what is the function of a receptor ?
receptors carry signals across cell membranes
51
functional proteins have ...
ligands
52
what is a ligand ?
a ligand is a molecule which binds to a protein
53
what can a ligand be ?
a ligand can be a substrate, co-factor or inhibitor of an enzyme
54
do enzymes increase of decrease the activation energy of a reaction ?
they lower the activation energy of a reaction which will increase the rate
55
enzymes catalyse reactions. this means ...
they speed up reactions without getting used up themselves
56
how do enzymes lower the activation energy of a reaction ?
they form a complex with the substrate to stabilise the transition state of the reaction
57
inhibition means that the enzyme works ...
less efficiently (the rate of the reaction is reduced )
58
ligands are typically signalling molecules like...
adrenaline, acetyl choline, histamine or seratonin but can be proteins
59
what is an ion channel ?
an ion channel is a type of receptor which can open, and allow ions to pass in or out of the cell, when the signalling molecule binds to it
60
part of the immune system produces antibodies. what are antibodies ?
antibodies are proteins designed to bind to a particular antigen
61
will antibodies bind to molecules which have a similar shape to their antigen ?
no- antibodies are very specific and will ignore molecules which are very similar but not identical
62
antibodies specificity is very useful in ...
biotechnology
63
most of the essential structure and function of a cell is mediated by a ...
protein
64
if the wrong protein is produced by faulty ..., or a protein is underexpressed, a ...
gene expression disease state can occur
65
what is one way disease can be caused ?
by exogenous proteins which cause other proteins to fold badly
66
what are exogenous proteins ?
exogenous proteins cause other proteins to fold badly
67
how is prion disease caused ?
it is caused by the incorrect folding of normal brain proteins called prions. this was due to proteins from infected meat.
68
can a mistake in the proteins primary structure have consequences on the secondary,tertiary and quaternary structure ?
yes and hence it would also affect protein function
69
many kinds of cancer are associated with faulty ... produced from faulty ...
proteins genes
70
what is cml disease ?
this is when an abnormal gene produces a protein which causes blood cell proliferation-too many white blood cells
71
polysaccharides are usually ... or ... molecules
structural storage
72
glucose is an ...
aldohexose
73
is glucose hydrophobic ?
no it is hydrophilic and H-bonds very well
74
what is the body's main energy substrate ?
if available it is glucose and the brain works on almist nothing else
75
how is excess glucose removed from the blood ?
it is removed from the blood by insulin and is stored as glycogen
76
is a lack of insulin in the blood dangerous ?
yes it is, without insulin, the blood level of glucose would reach dangerous levels .
77
what is usually used for a diagnosis of diabetes ?
glucose in urine and high levels of glucose in the blood
78
how do we find out if there is elevated levels of glucose in the urine ?
a simple dipstick will show whether elevated levels of glucose are present
79
to see if there are high levels of glucosse in the blood we would ...
do a diagnostic test which is based on glucose oxidase, an enzyme, but monitoring also utilises hemologin glycation
80
what is the definition of lipids ?
lipids are a heterogeneous, diverse group of molecules typified by their insolubility in water
81
fats and oils are used in
storage
82
phospholipids and cholstrol are found in
membranes and lipoproteins-structural
83
how are triacylglycerols (fats) converted into energy ?
they are broken down into free fatty acids by the enzyme lipase
84
cell membrane lipids have a ... ... at the end
polar group
85
what does cholstrol do ?
it is found in membranes and rigifies the bilayer membranes
86
what does vitamin e do in the cell membranes ?
alpha-tocopherol is the main antioxidant in cell membranes it prevents the peroxidation of polyunsaturated fatty acyl chains in lipids