building blocks of bio Flashcards

1
Q

water accounts of __% of a cell’s weight

A

70%

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2
Q

name the four building blocks of every cell

A

sugars
fatty acids
amino acids
nucleotides

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3
Q

polymers made from the four building blocks

A

sugars –> polysaccharides
fatty acids –> fats / lipids / membranes
amino acids –> proteins
nucleotides –> nucleic acids

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4
Q

basic structure of a nucleotide

A

N-containing base
5-C sugar
phosphate group(s)

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5
Q

name five types of N-containing bases

A

adenine
guanine
cytosine
thymine
uracil

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6
Q

how many rings do each of the N-containing bases have?

A

A and G = 2
T and C = 1
so that all base pairs have 3 rings in total

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7
Q

nucleoside vs nucleotide

A

nucleoside = sugar + base
nucleoTide = sugar + base + phosphaTe (eg. ATP, dAMP)

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8
Q

biological polymerisation is driven by___

A

ATP
w/ loss of H2O (condensation polymerisation)

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9
Q

general bonding in DNA

A

covalent - phosphate backbone
H-bonds between bases

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10
Q

DNA structure main features

A

double helix, major + minor groove
phosphate backbone = POLAR due to -vs charge on phosphate
planar bases
stacking of bases influences stability

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11
Q

how many H-bonds form between A-T and C-G?

A

A=T
C-G 3 bonds

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12
Q

RNA vs DNA nucleotides differences

A

additional hydroxyl group in ribose sugar of RNA (ribose, not deoxyribose)
Uracil rather than thymine

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13
Q

describe RNA secondary structure

A

does not form a double helix like DNA
moves in space until it finds the lowest energy folding combination
held together by H-bonds

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14
Q

general amino acid structure

A

NH2 amino group
COOH carboxyl group
R functional group (side chain) attached to alpha C chiral centre

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15
Q

at pH7, what happens to amino acids?

A

both amino and carboxyl groups ionised –> zwitterionic

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16
Q

formation / breaking of peptide bond

A

N and C terminus of two amino acids
condensation reaction –> peptide bond
hydrolysis reaction (+H2O) to break

17
Q

describe the four levels of protein structure

A

primary = amino acid residues
secondary = local folding (determined by interactions between amino acids)
tertiary = global folding, combination of secondary structures –> polypeptide chain
quaternary = assembled subunits

18
Q

describe the bonding in an alpha-helix protein secondary structure

A

N-H of every peptide bond is H-bonded to the C=O four amino acids away
Left or right handed

19
Q

bonding in beta-sheets of protein

A

H-bonding between adjacent strands of polypeptide chains
can run parallel / antiparallel

20
Q

simple monosaccharide general formula

A

(CH2O)n
eg. glucose C6H12O6

21
Q

how are disaccharides formed

A

C w/ ald/ket can react w any hydroxyl group on a second sugar
glycosidic bond formed
eg. sucrose = glucose + fructose

22
Q

what is a glycosaminoglycan

A

GAGs = unbranched polysaccharide chains made of repeating disaccharide units

23
Q

name 5 GAGs

A

hyaluronic acid
chondroitin sulfate
dermatan sulfate
heparin sulfate
keratan sulfate

24
Q

describe the properties of GAGs

A

polysacc chains are stiff + strongly hydrophilic
–> GAGs occupy huge volume relative to mass + negative charge density attracts could go cations, esp Na+ which is osmotically active sucking up lots of water
hence GAGs fill extracellular space

25
Q

phospholipid molecule structure

A

hydrophilic head (glycerol+phosphate+polar functional group)
two hydrophobic fatty acid tails which can be saturated or unsaturated

26
Q

lipid micelles are formed from…

A

phospholipids w a single tail, form a ball

27
Q

cholesterol structure

A

rigid steroid ring + polar head group = hydrophilic
non polar hydrocarbon tail
amphipathic

28
Q

cholesterol function

A

stiffer than phospholipids, can pack into membranes –> controls stiffness
important in cell signalling