Biological Molecules Flashcards

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1
Q

Monomer

A

small units that from basic units of life

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2
Q

Polymer

A

made up of monomers. can be long simple strands or highly branched

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3
Q

monomers
glucose
amino acids
nucleotide

A

polymer
cellulose/ starch/ glycogen
protein
DNA/ RNA

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4
Q

condensation reaction

A

a molecule of water is removed when monomer to polymer

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5
Q

hydrolysis

A

breaking a bond by adding water

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6
Q

monosaccharides

A

single simple sugars e.g glucose, fructose

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7
Q

polysaccharides

A

multiple monosaccharides

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8
Q

glucose polysaccharides- glycogen

A

-made from alpha glucose
-found in animals
-highly branched
-used for storage

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9
Q

Glucose polysaccharides- cellulose

A

-made form beta glucose
-found in plants
-parallel, long single chains
-hydrogen bonds cross link
-used for cell wall strength

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10
Q

glucose polysaccharides- starch

A

-made from alpha glucose
-found in plants
-highly branched
-used for storage

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11
Q

structure bonds

amylose

A

helically coiled 1-4 bonds

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12
Q

structure bonds

amylopectin

A

branched 1-6 bonds, more soluble

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13
Q

starch

A

-helical/ spiral shape so compact
-large/ insoluble so osmotically inactive-does not effect water potential
-branched so glucose is easily released for respiration
-large so cannot leave the cell

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14
Q

cellulose

A

long, straight, unbranched chains of beta glucose joined by hydrogen bonding to from microfibrills which provides rigidity and strength

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15
Q

lipids

A

lipids contain c,h,o bbut less oxygen
lipids are non polar molecules so are insoluble but soluble in organic solvents e.g ethanol
they do not form polymers

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16
Q

triglycerides

A

lipids made from 1 glycerol and 3 fatty acids

17
Q

saturated fats

A

each carbon atom in the hydrocarbon chain has 4 other atoms bonded to it makes them solid and room temperature
straight chains which allow them to lie close together

18
Q

unsaturated

A

have double bonds between carbon atoms in the hydrocarbon tail this make them liquid at room temperature

19
Q

oils solid liquid

triglycerides with double bonds

A

they tend to be oils the ‘kink’ prevents the chains getting close together meaning they are liquids

20
Q

hydrophilic

A

attracted to and interacts with water but not with fats

21
Q

hydrophobic

A

not attracted to water/ repels water but can mix easily with fats

22
Q

triglyceride characteristics

A

-glycerol
-3 fatty acids
-no phosphate group
-non polar
-whole molecule
-hydrophobic
-soluble in lipids

23
Q

phospholipids characteristics

A

-glycerol
-2 fatty acids
-phosphate group
-polar
-hydrophobic tail
-hydrophilic head
-soluble in water

24
Q

proteins eg

A

-enzymes
-haemoglobin
-antibodies
-hormones
-muscle fibres
-antigens

all of them have a specific shape

25
Q

how many amino acids exist naturally

A

20

26
Q

primary structure proteins

A

number, type and sequence of amino acids
linear chain joined with peptide bonds

27
Q

secondary structure

A

alpha helices and beta pleated sheets formed by hydrogen bonds

28
Q

tertiary structure

A

3d folded amino acids by hydrogen and ionic bonding or disulphide bridges to form globular proteins

29
Q

quaternary structure

A

has 2 or more polypeptide chains

30
Q

proteins definition

A

polymer chain of amino acids joined by peptide bonds from a condensation reaction

31
Q

describe the structure of proteins TAT

A

polymer chain of amino acids joined by peptide bonds from a condensation reaction. the primary structure is the number, type and sequence of amino acids. the secondary structure are alpha helices and beta pleated sheets formed by hydrogen bonds. the tertiary structure is 3d folded amino acids by hydrogen and ionic bonds and disulphide bridges. the quaternary structure is 2 or more polypeptide chains.

32
Q

Induced fit model

A

Shape of active site changes as substrate binds. stressing/distorting/ bending/ applying pressure to the bonds which lowers the activation energy when the enzyme-substrate complex forms.

the shape of the active site is complementary.

33
Q

Enzyme inhibitors

A

a substance that directly or indirectly interferes with the functioning of the active site of an enzyme so reducing enzyme activity.