Macromolecules Flashcards

1
Q

Roles of sugars and polysaccharides

A

Food molecules and energy store
Structural support
cell protection
cell-cell adhesion and motility
cell signalling

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2
Q

What are D isomers

A

straight chain polyhydroxy alcohols (linear form of cyclic sugars)
either an aldehyde or ketone group
at least three carbon units

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3
Q

What are the two glucose enantiomers

A

alpha and beta glucose

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4
Q

How do the two glucose enantiomers differ, which one is more stable

A

alpha glucose = OH group pointing down
beta glucose = OH group pointing up

beta is more stable as OH groups are further apart in the molecule

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5
Q

What are the polymers of the glucose enantiomers

A

alpha = starch and glycogen
beta = cellulose and chitin

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6
Q

How are sugars linked

A

condensation reaction, removing water forming a 1,4 glycosidic bond

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7
Q

What is the reducing end

A

the end that is free to become linearised

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8
Q

Glycogen

A

highly branched glucose polysaccharide
branching increases the number of ends available to be digested for rapid release of glucose

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9
Q

Structure of a ribosome

A

RNA and protein
active site of ribosome is RNA which is the catalyst for protein synthesis
ribozyme - extra OH on ribose

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10
Q

Structure of a ribosome

A

RNA and protein
active site of ribosome is RNA which is the catalyst for protein synthesis
ribozyme - extra OH on ribose

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11
Q

What is DNA and RNA used for

A

DNA = store of genes
RNA = gene expression

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12
Q

What bonds form when nucleotides are polymerised

A

phosphodiester

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13
Q

What type of pentose is deoxyribose and where is it deoxy at

A

Aldopentose
deoxy at the 2 position

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14
Q

How many hydrogen bonds between A and T, C and G

A

A and T = 2
C and G = 3

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15
Q

What are purine and pyrimidine bases

A

Purine = A and G, two rings
Pyrimidine = T, U, C, one ring

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16
Q

Why does a purine and pyrimidine always complementary base pair

A

keeps the sugar phosphate backbone the same distance apart all the way along the DNA strand

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17
Q

what is a nucleoside

A

ribose and base

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17
Q

what is a nucleoside

A

ribose and base

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18
Q

Which complementary base pair requires less energy to break

A

A and T as there is only two hydrogen bonds between them

18
Q

Which complementary base pair requires less energy to break

A

A and T as there is only two hydrogen bonds between them

18
Q

Which complementary base pair requires less energy to break

A

A and T as there is only two hydrogen bonds between them

18
Q

Which complementary base pair requires less energy to break

A

A and T as there is only two hydrogen bonds between them

19
Q

Levels of protein structure

A

Primary = the order of amino acid residues in the chain
Secondary = localised regular arrangements of the polypeptide backbone to form alpha helices and beta sheets
Tertiary = overall three dimensional fold of the protein
Quaternary = arrangement of multiple amino acid chains

20
Q

Amino acids

A

Chiral carbon molecules
Carboxyl group
Amino group
Hydrogen
R group

Only amino acid that is not chiral = glycine

21
How do amino acids differ
Chemical groups within side chains
22
Hydrophobic
Water hating Large and non polar R groups Cluster away from water in the core of the protein or at interaction interfaces
23
What are the hydrophobic Amino acids
Alanine Valine Leucine Isoleucine Glycine Cysteine Phenylalanine Tryptophan Proline
24
Which two hydrophobic amino acids contain sulphur
Cysteine Methionine
25
What amino acid can form disulphide bonds and how
Cysteine In an oxidising environment so not in cells as this is reducing
26
Hydrophilic
Water loving Forms hydrogen bonds with water Can be uncharged but polar, negatively charged, positively charged
27
What are the negatively charged amino acids
Aspartic acid Glutamic acid (Both carboxylic acids)
28
What are the positively charged amino acids
Lysine (primary amine) Arginine Histidine
29
What are the uncharged polar amino acids
Serine Threonine Tyrosine (Hydroxyl groups) Asparagine Glutamine
30
Peptide bond
Condensation reaction removing water as the amino and carboxyl groups are joined together forming a linear peptide
31
How are proteins numbered
From the N terminus to the C terminus Residue 1 has a free NH3 +
32
What are the side chains of the polypeptide
The R groups
33
What structure is a peptide bond
Planar - no rotation (All in one plane)
34
Why can the peptide bond flick between single and double bonded
Delocalisation of electrons from the nitrogen onto the single C-N gives it a partial double bond characteristics Restricts rotational movement of the polypeptide chain around that bond
35
How is the confirmation of the backbone describe by
Torsion angles
36
What are the angles of rotation
Phi = angle around alpha carbon and nitrogen Psi = angle around alpha carbon and carbon
37
How does folding of the polypeptide chain occur
Rotation of the phi and psi angles for each residue Rotation around alpha carbon is not completely free as many combinations of phi and psi angles cause steric clashes of side chains
38
Disaccharides
Maltose = alpha glucose and alpha glucose Sucrose = alpha glucose and alpha fructose Lactose = alpha glucose and beta galactose Lactulose = beta galactose and beta fructose
39
Consequences of breaching in starch and glycogen
Starch is more densely packed More exposed end units for access by glycogen synthase/phosphorylase
40
How can C be converted to U
Spontaneous deamination
41
Why is DNA double stranded
Provide copying mechanism Enable repair of damaged bases Stabilise with hydrogen bonds
42
Why is RNA single stranded
Allow protein synthesis Allow internal hydrogen bonding Allow binding to proteins as well as other RNAs
43
Ramachandran plot shows
Most optimal phi and psi angles to avoid steric clashes