Biological molecules Flashcards

1
Q

are h-bonds strong ?

A

no

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2
Q

liquid water explanation ( h-bonds and b.p?)

A

molecules h-bond together creating high b.p as h2o bonded together and therefore cant escape as gases easily

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3
Q

Ice explanations hydrogen bonds and strenght

A

less movement as less KE

more h-bonds form less break

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4
Q

H-bonds and temp changes

A

h-bonds in water (liquid) hold H2O molecules= restrict movement. lots of energy needed to increase temp, keeps lakes stable
evaporation of H2O = lots of energy and removes heat

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5
Q

which is denser. Ice or H2O

A

ice i sless dense. allowing it to float on top, ie iinsulating layer on lakes

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6
Q

droplet shape of water?

A

help by h-bonds, giving shape. Cohesion

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7
Q

what allows something to be soluble?

A

balanced bonds, h - bonds

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8
Q

water is a large ________________________ in the body

A

transport median

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9
Q

Acid and amine group in amino acid?

A

amine group = H\ N
H/
acid = c=o
\OH

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10
Q

amino acid formula

A

NH2CHRC=OOH

Diagram

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11
Q

Bonding of amino acids

A

condensation reaction - H2O produced.

OH + H bond = bond between C-N occurs

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12
Q

reverse of condensation =

A

hydrolysis

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13
Q

protein primary structure

A

specific sequence of amino acids

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14
Q

secondary structure

A

refers to coiling and pleating of parts of polypeptide molecule:
either alpha helix or beta pleated sheet
h-bonds hold coil in place theyre weak but there a re lots so = strong!

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15
Q

Tertiary structure

A

overall 3D structure of final protein molecule

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16
Q

tertiary deeper

A

coils/ pleats often with straight runs of amino acids between. many types of bonding/interactions occur;
disulfide bonds
ionic bonds
hydrogen bonds
hydrophobic + hydrophilic interactions.
specific to protein function ie hormone must be specific to fit hormone receptor of a target cell

17
Q

quaternary structure

A

some proteins made up of more than one polypeptide subunit joined together. eg; haemoglobin + insulin

18
Q

structure of haemoglobin

A

transport protein
consists of 4 polypeptide subunits ( 2 alpha and 2 beta)
a water soluble globular protein

19
Q

function OF HAEM

A
carry O2 from the lungs to the tissues
haem group contains Fe2+ ion 
haem group = colour (purple +oxy --> Bright red) 
O2 binds to haem, 4 max 
haem = prosthetic group
20
Q

collagen structure

A

fibrous structural protein
3 polypeptide chains wound together like a rope
1 chain is coiled and made from 1000 amino acids
hydrogen bonds between chains form (giving strength)
also each collagen molecule foroms covalent bonds (cross links) between other collagen molecules ( resulting in a collagen fibric. many = collagen fibre)

21
Q

function of collagen

A

provides strength
eg in the walls of arteries
bones formed from collagen
cartilage and connective tissues

22
Q

alpha glucose : ( monosacharides ) 3 things

A

soluble in H2O
form crystals
are sweet
DIAGRAM (6 one off 5. O at 6 and H above OH for alpha (beta swap))

23
Q

joining monosaccharides + splitting disaccharides

A

condensation reaction
reverse = hydrolysis ( glysocsidic bonds)
OH + H = H2O

24
Q

2 alpha- glucose bonded form disacharide caleed

25
starch structure:
mixture of long, straight-chain amylose & branched amylopectin alpha glucose energy store- can be broken down into glucose molecules insoluble
26
cellulose
beta glucose polymer chain h-bonds between monomers crosslinked by h-bonds to form microfibrils h-bond again --> macrofibrils ebedded with polysaccharide glue of substances called pectins
27
trigylceride molecule = | and how they bond
1 glycerol molecule bonded to 3 fatty acids condensarion reaction = ester bond theyre insoluble and hydrophobic
28
phospholipid
glycerol molecule, 2 fatty acid chains and phosphate group phosphate head = hydrophilic fatty acid tail hydrophobic
29
whats a triglyceride funstionans solubility
compact negery store. insoluble in water so doesnt affect w.p
30
phospholipid function
forms a molecule which is part hydrophobic and part hydrophilic. idea for membranes
31
cholesterol structure andfunction
4 carbon - based ring structure | fors a small thin molecule that fits into lipid bilayer giving strength and stabilitly
32
food test for reducing sugar;
benedicts test; heat with benedicts solution ( alkaline copper sulfate) blue --> orange-red ( precipitate) eat to 80degrees in H2O bath
33
food test for starch
add iodine solution | brown --> blue/black
34
non- reducing sugar food test
benedicts test - doesnt work boil with HCl, then cool + neutralise with sodium hyrdrogen carbonate solution/ sodium carbonate solution, then repeat beneditcts blue --> orange/ red
35
protein
add biuret reagent | blue to lilac
36
lipid test
add ethanol to extract (dissolve) lipid and pour alcohol into water ina nother test tube white emulsion forms near top of water
37
colorimeter
after benedicts test the more light shone through blue liquid the more glucose was present THINK
38
Hydrogen bonding what is it
negative part of a molecule bonds to h+. must aksi have lone pair eg; H2O