biological molecules Flashcards

1
Q

Describe the induced-fit model of enzyme action

A

Substrate binds to the active site/enzyme,
Active site changes shape (slightly) so it is complementary to
substrate, Reduces activation energy

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2
Q

what is dna made up of

A

deoxyribose sugar, phosphate group and a nitrogenous base

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3
Q

what is rna made up of

A

ribose sugar, phosphate group and a nitrogenous base + uracil

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4
Q

what is a monomer

A

a smaller repeating unit used to make up larger molecules

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5
Q

what is a polymer

A

a larger repeating unit made up of lots of monomers joined together by a condensation reaction forming a glyosidic bond

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6
Q

what is a monosaccharide

A

a unit of sugar called saccharide used to make up larger molecules

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7
Q

what is a polysaccharide

A

larger unit of sugar made up of many monosaccharidic units joined together

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8
Q

a glucose

A

hydroxide on the bottom, h on the top

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9
Q

b glucose

A

hydroxide group on the top, hydrogen on the bottom

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10
Q

properties of starch

A

made up of a glucose arranged in a helix, chains may be branched or unbranched. Unbranched chains form a tight coil, making the molecule useful for storage.
- insoluble, doesnt affect water potential
- can be readily hydrolysed into a glucose for respiration

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11
Q

properties of glycogen

A

made up of a glucose joined by 1-4 and 1,6 glyosidic bonds. Branched chains
insoluble, compact, enzyme action

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12
Q

properties of cellulose

A

made up of b glucose monomers joined by 1,4 glyosidic bonds, straight unbranched chains that run parallel to each other, hydrogen bonds able to form cross linkages that form microfibrils, providing strength and rigidity to cells

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13
Q

how are the disaccharides formed

A

maltose - glucose + glucose
sucrose - fructose + glucose
lactose - galactose + glucose

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14
Q

amylopectin structure

A

isomer of starch, made up of glucose molecules joined by 1,4 and 1,6 glycosidic bonds
branched
compact,

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15
Q

amylose

A

unbranched chain of glucose molecules, isomer of starch.
compact and coiled.

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16
Q

tertiary level structure of proteins

A

disulphide bridges, hydrogen bonds and ionic bonds
3D shape of a protein formed from twisting and folding

17
Q

globular vs fibrous proteins

A

globular - compact
fibrous - long and can be used to form fibres

18
Q

primary structure of proteins

A

order and number of amino acids in a sequence

19
Q

secondary structure of proteinsar

A

chain of amino acids that either make alpha helix or beta pleated sheet
hydrogen in the NH has a slight negative charge whilst the C—O has a slight positive charge forming weak hydrogen bonds that ca either form alpha helix or beta pleated sheet

20
Q

quaternary level structure

A

large proteins form complex molecules containing different numbers f polypeptide chains. non protein groups
3 polypeptide chains associated with the molecules