carbohydrates and proteins Flashcards

(46 cards)

1
Q

what are the simplest carbohydrates ?

A

monosaccharides/sugar monomers

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2
Q

can the carbon skeletons of monosaccharides vary in length ?

A

yes

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3
Q

what makes monosaccharides useful ?

A

they are the main fuel for cellular work
used as raw materials to manufacture other organic molecules

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4
Q

whats the name for monosaccharides with only three carbons ?

A

trioses

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5
Q

whats the name of monosaccharides that have 5 carbons ?

A

pentoses

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6
Q

whats the name of monosaccharides that have 6 carbons ?

A

hexoses - these are also structural isomers

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7
Q

what are the 3 common disaccharides ?

A

sucrose, lactose and maltose

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8
Q

what do we know about sucrose ?

A

is table sugar and is also used in plants as the molecule to transport sugar around

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9
Q

what do we know about maltose ?

A

found in seeds like wheat or barley and produced as part of the breakdown of starch to glucose

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10
Q

what do we know about lactose ?

A

is milk sugar

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11
Q

what are glycosidic bonds ?

A

they are covalent bonds that form between a carbohydrate and another molecule

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12
Q

what can polysaccharides function as ?

A

storage molecules or structural compounds

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13
Q

are polysaccharides usually hydrophilic or hydrophobic ?

A

hydrophilic

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14
Q

what are the biologically important polysaccharides ?

A

starch, glycogen, cellulose, chitin

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15
Q

what are the features of starch ?

A

is composed of glucose monomers
used by plants for energy storage

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16
Q

what are the features of glycogen ?

A

composed of glucose monomers
used by animals for energy storage

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17
Q

what are the features of cellulose ?

A

is a polymer of glucose
forms plant cell walls

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18
Q
A
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19
Q

what version of glucose does cellulose have ?

20
Q

what version of glucose does glycogen have ?

A

alpha version

21
Q

what are the features of chitin ?

A

used by insects and crustaceans to build an exoskeleton
found in the cell walls of fungi

22
Q

the hydrolysis of storage polysaccharides such as glycogen, release glucose when …

A

energy demand is high

23
Q

do glycogen stores last long ?

24
Q

in human how long would it take for the glycogen store to be depleted without food ?

25
what do enzymes do ?
serve as catalysts and regulate virtually all chemical reactions within cells
26
what bonds link amino acid monomers together ?
peptide bonds
27
how are peptide bonds formed ?
through dehydration reactions joining the carboxyl group of one amino acid to the amino group of the next amino acid
28
side chains can be ...
hydrophobic (greasy and lipophilic) h-bonding (more polar and hydrophilic) charged (either negative positive, polar and hydrophilic)
29
what do we know about hydrophobic side chains ?
all of these side chains are greasy and would break up the h-bonding network of water. they are lipophilic and very happy in a cell membrane
30
what do we know about h-bonding side chains ?
all of these can act as h-bond donors or acceptors. this makes them much more hydrophilic and less lipophilic. they can also interact with other parts of the protein chain
31
what do we know about positively charged side chains ?
all of these side chains will be protonated at a physiological ph. they can also h-bond as well as being attracted to negative charges, and they are polar.
32
what do we know about negatively charged side chains ?
these have a carboxylic acid in their side chain which will be largely deprotonated at a physiological ph. this makes them polar, hydrophilic/lipophobic and attracted to positive charge
33
what is the primary structure ?
the sequence of amino acids in a polypeptide chain
34
what is secondary structure ?
the formation of secondary structures such as alpha helices and beta pleated sheets -these form because of hydrogen bonding between different amino acids in the chain
35
what is tertiary structure ?
when the secondary structures fold up to form a very precise three dimensional structure
36
what are the forces responsible for the formation of tertiary structure ?
hydrogen bonds ionic bonds disulphide bonds van der waal's forces
37
what can split hydrogen bonds ?
high temperatures and an altered pH
38
how can ionic bonds be split ?
by changing the ph
39
how can disulphide bonds be split ?
by reducing agents
40
what are van der waals forces ?
these are weak forces of attraction between non-polar groups .
41
how are van der waal's forces split ?
split by a rise in temperature
42
what are the features of fibrous proteins ?
fibrous protein molecules form long chain or fibres their fibrous nature makes them insoluble in water and this makes them useful for structure and support
43
what is the structure of fibrous proteins ?
fibres form a triple helix of polypeptide chains these chains are held together by hydrogen bonds
44
if a proteins shape is altered, it can no longer ...
function
45
what happens to a protein in the process of denaturation ?
it unravels loses its specific shape and loses its specific function
46
what can denature proteins ?
by changes in salt concentration, changes in pH, or high heat