intro to biomolecules Flashcards

1
Q

rutherford atom

A

nucleus => protons/ neurtrons have weight

protons = + charge
electrons = - charge => no particular weight

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2
Q

shells of atom + stability

A

full shell = stability
1st shell = 2
2nd = 8
atoms can donate electrons to neighbouring atoms that are missing electrons => electrostratic attraction => holds structure together and its relatively stable
not a very strong bon d= falls apart in water

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3
Q

what feature of water molecules enables ionic substances to dissolve in water

A

water molecules are polar and are attracted to the + and - ions surrounding them

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4
Q

maintaining ion concentrations

A

if u remove red blood cell from blood

must suspend it in solution = isotonic => same sort of concentration as extracellular fluid

if too low => cell swells and explodes

too much = shrunken

ionic concentrations must be even between two sides of cell

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5
Q

covalent bonds

A

Sharing electrons

Can be one from each partner or more
Determines the shape of the molecule
Stronger than ionic bond

takes more energy to break

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6
Q

what statement is true of covalent bonds

A

Atoms find the ideal separation distance where the electrostatic forces are maximal

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7
Q

polar bonds

A

not all electrons are shared equally
parts of the molecules are more negatively charged
electrostatic interactions

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8
Q

sugars

A

same structure => 1 carbon 2 hydrogen 1 oxygen
adopts different shapes => can’t all be recognised by the same enzyme
source of energy of cell

can be joined together => condensation reaction => binds the two together or hydrolysis => break it down to give us energy

can be stored <=> glycogen
stored in muscles + liver => depends on how rapidly you need to access it

liver => break down + generate glucose + supply in other parts of the body

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9
Q

why are some fats described as saturated

A

fatty acid chains are saturated with hydrogen

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10
Q

fatty acids

A

saturated = have no double bonds / unsaturated = have one or more double bonds in hydrocarbon tail => double bond is rigid and creates a kink in the chain => other half rotates
=>
hydrophilic/ hydrophobic => amphipathic
carboxyl group at end makes it = negative charge =>
head = hydrophilic
fatty acid tails = 2 => hydrophobic

can be stored as triacyl glycerol that can be converted into energy => ester linkage to glycerol to form triacylglycerols = triaglycerides

important member of cell membranes ]

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11
Q

steroids

A

4 fused carbon rings
functional groups attached
derived from cholesterol

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12
Q

amino acids

A

building block to make protein
carbon, carboxyl grp + amino grp on other side and diff side chains
polymerise them to generate a peptide bond
source of energy => conversion
can be used as neurotransmitters
used to make other molecules

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13
Q

nucleotides

A

carbon nitrogen ring which is bound to a sugar that then has phosphates on it.
short term store of energy => ATP
alot of energy stored between 3 phosphates esp 2 and 3
stores of electrons => NAD/NADP = reducing store for biosynthesis or ATP reduction

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14
Q

nucleoside

A

carbon nitrogen ring which is bound to a sugar

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15
Q

3 dimensional structure

A

hydrophobic regions in the middle of the molecule and to have the hydrophilic parts on the outside.

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16
Q

pepsin works in stomach, how does it maintain activity in low pH

A

its active site deep in the structure

17
Q

diff between blood types + vaccines manufacturers

A

difference between the different blood types is because of sugars that are attached to lipids on the surface of the red blood cell.

enzymes in the immune system can recognise these relatively subtle differences => exploited by viruses, viruses, if they want to get into our bodies.
They have lots of sugars on the outside and they change the sort of sugar structure quite easily = diff

18
Q

change in structure can

A

disrupt function