biomolecules Flashcards

1
Q

what are monosaccharides?

A

the basic unit of carbohydrates, made of carbon,hydrogen and oxygen atoms

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2
Q

what is the general formula of carbohydrates?

A

(CH2O)n
n can be 3,5 or 6,they can be classified according to the number of carbon atoms in the molecule
n=3-trioses n=5-pentoses n=6-hexoses e.g fructose, glucose,galactose

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3
Q

what are disaccharides?

A

-disaccharides is what is formed when two monosaccharides are joined together e.g glucose+ fructose=sucrose

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4
Q

what is a dehydration/condensation reaction?

A

a reaction where water is release, energy is required

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5
Q

what is a glycosidic bond?

A

a bond that holds two monosaccharides together

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6
Q

what is condensation polymerisation?

A

a serious of condensation reactions that add units together until very large polysaccharides are formed

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7
Q

what do the properties of a polysaccharide depend on?

A

solubility
-the length
-the extent of branchinng(weather the units are being added to the side of the chain or its ends)
-whether the chain is straight or coiled

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8
Q

compare normal haemoglobin to glycated haemoglobin…

A

-normal haemoglobin transports 4 oxygen molecules by binding to 4 iron atoms inside each haem group while glycated haemoglobin permanently binds to proteins like haemoglobin after prolonged exposure to elevated blood sugar

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9
Q

what are the different types of lipids?

A

-saturated fats
-unsaturated fats-carbon-carbon double bond
-cis saturated fats
-trans-unsaturated fats

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10
Q

what are the two types of unsaturated fats?

A

-monounsaturated-single double bond
-polyunsaturated-multiple double bonds

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11
Q

what are cis unsaturated fats?

A

-usually naturally occurring fats where the hydrogens are on the same side of the double bonds and this creates a kink these fats are likely to be a liquid at room temp

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12
Q

what are trans-unsaturated fats?

A

-manufactured fats where the hydrogens are on opposite sides of the double bond, there are no kinks and these fats are likely to be solid at room temp
-they are associated with cardiovascular diseases

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13
Q

why are saturated and trans fats bad?

A

they increase the LDL levels in the blood and this is associated with heart disease

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14
Q

why are unsaturated fats good?

A

-they help reduce LDL levels in the blood and so this decreases the cholesterol to HDL ratio helping take cholesterol to the liver where it can be disposed

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15
Q

what is cholesterol?

A

-a lipid which is amphipathic, it is an essential component of cell membranes and it came before steroids, vitamin D and bile acids

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16
Q

define amphipathic…

A

-having both hydrophobic and hydrophilic regions

17
Q

how is cholesterol transported?

A

-by lipoproteins

18
Q

what is HDL and LDL?

A

-HDL-good cholesterol trasported to the liver for recycling
LDL-bad cholesterol-accumulates in the inner wall of the arteries

19
Q

what are phospholipids?

A

-lipids that are amphipathic with a hydrophilic head and hydrophobic tail and are joined by glycerol
-they form bilayers e.g the cell membrane

20
Q

what are proteins?

A

-they are built on monomer units called amino acids and interact with each other and other biological macromolecules to form assemblies
-there are 20 amino acids, they are zwitterions at a neutral pH and are amphoteric

21
Q

define amphoteric…

A

can react both as a base and an acid

22
Q

what is the structure of a protein?

A

-an amine NH2
-a carboxyl (COOH) functional group
-a side chain (R group) specific to each amino acid

23
Q

how can we classify amino acids by their R groups?

A

-Non-polar have hydrophobic R-groups
-Polar have hydrophilic r-groups
-Acidic have negatively-charged R groups
-basic have positively-charged R groups

24
Q

define hydrophobic and hydrophilic…

A

-hyrophobic-does not dissolve in water
-hydrophillic-tendency to interact with water at a biological pH

25
what are amino acids?
compounds that contain amine (NH2) and carboxyl functional groups with a side chain(R-group) specific to each amino acid
26
what is the primary structure of proteins?
sequence of amino acids in a peptide or protein
27
what is the secondary structure of a protein?
3 dimensional form of local segments of proteins e.g alpha helix,beta pleated sheet
28
what is the tertiary structure of proteins?
-the 3-dimensional shape,amino acid side chains which may interact and bond in different ways,the interactions and bonds of the side chain within the protein determine its tertiary structure
29
what is the quaternary structure of proteins?
-the number and arrangement of multiple folded protein sub units in a multi-subunit complex
30
what is a proline residue?
a chain breaker that can facilitate a change in the direction due to the amino and carboxyl group being fixed within a ring
31
what is a cofactor?
-a non-protein molecule required by enzymes for catalytic activity (apoenzyme vs holoenzyme) E.g P450 enzymes metabolize drugs by using a haem cofactor that binds oxygen
32
what are the methods used to study proteins?
-Mass spec for the primary structure x -ray crystallography for the secondary,tertiary and quaternary structure