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Chapter 3 Flashcards

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1
Q

Atoms in each

A

Carbidygate = cho
Lipids = cho but more quantity in one
Proteins = amino acids = c hydrogen oxygen, but nitrogen for amino group, and soulful in disuflide bdiges
Nucleus acids = cho, nitrogen and phosphorus (phosphate backbone)

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2
Q

How are hydrogen bonds made

A

Some bonds have electrons unevenly distrubutir fur to electrongstivity differences m which maked those bonds polar with slightly partially positbe and negative charged

When polar bonds interact with each other they form hydrogen bonds which sre stronger than normal intermoeluclsr

Hydrogen bond is (relatively weak ) interaction between partially negative atom’s lone pair and a partially positive hdyroen atom

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3
Q

All anomalous oropetiesof water as a result

A
  • high SHC and LATEN HEAT VAPORIETWITOOM
  • ICE less dense than liquid water
  • surface tension
  • cohesive and adhesive properties
  • ## can act as a solvent
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4
Q

Why does water have a high latent heat of vaporisation and why specific

Insane reason for coolant 2

A
  • hydrogen bonding between molecules of water means more energy needed to overcome these bonds, and thus boiling point and SHC is higher p
    And latent heat higher too, more energy to increase temp of 1kg water to 1k

Useful

1) act as a coolant 2 ways
- buffers temperature changes during chemical reactions in cells where energy is released due to having high SCH, thus temoertaure here kept constant and this is useful for things like enzumss who could dneature if temp increased
- to cool organisms, animal release like sweat and as it has high latent heat a lot energy is removed when it evaporates, animals and plants in transportation too

THIS MEANS KESS ENERGY MUST BE USED ON TEMPERATURE CONTROL

2) maintains constant environment -
- high SHC and latent heat mends the temperature in oceans etc are relatively constant and that the water won’t evaporate easily, this means there is a constant habitat for them to live in

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5
Q

Why more dense

Use (2)

A

Below 4° the hydrogen bonds hold water molecukes in an open lattice , so that they are in fixed positions, meaning they held further apart on aggregate then wentn they are liquid, meaning more volum for same mass and less density

  • as it is less dense, it freezes from top bottom rather than other way, and as a result it creates an INSUKATING layer on top which means water underneath doesn’t freexe, and this allows awaits it canimals to survived
  • also a habitat
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6
Q

Cohesive and adehsifen

A

As water molecules attracted to each other due to hydrogen bonds they move as in mass and this is cohesion

As they also can form polar bonds with other materials they have adhesive properties .

It is for this reason if cohesion and adhesion that water can be drawn up a straw or plants by capillary action against gravity

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7
Q

Surface tension

A

This is because attractive scohedive sticks to itself more than with air, creating a SKIN of surface tendioj
This can provide a habitat for pindkaters etc

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8
Q

Why is it a solvent and why is this useful

A

It is ad solvent because it forms binds evilly with inorganic ionsnetc , this produced enough energy to break the predigesting bonds and thus it can dissolve these substances , so it tpdoes this to most polar etc

Acts as a transport medium in this case, can transfer ions etc out the body and in
So chemical medp

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9
Q

So what two mediums is what’re

A

Reaction medium and trwnsportn

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10
Q

So summary

A

SHC latent heat
- act as coolant through chemical buffer and also sweat
- this means LESS ENERGY ON ENERGY CINTROL
- constant environment AS WARER m doesn’t evaporate tinged etf
Density
- provided habitat
- freeze top bottom creating layer insulated
Surface tension
Cohesion adhesion
- moved as one mass as attracted to each other but also attracted to durfaces this means water can be drawn up against gravity = capilairy ,
Solvent
- solvent to many solutes like inorganic ions and also polar oned, transport medium to transport ijntinthrn cells and out from cells as wadteen

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11
Q

What is monosaccharide

A

Single unit of csrbidhyrste l disaccharide two and only more

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12
Q

Glucose

A

6 carbine make it a heroes monsachidre due to having 6 carbons with two vwirostiond alpha and beta glucose

Soluble in water and polar due to hydro cycle groups, soluble because of oh

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13
Q

Why is soluble impotent

A

Can dissolve into cytoplasm of cell

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14
Q

Beta glucose and alpha glucose

A

Beta beta do follow rule, up down up down

Alpha doesntso down down up down

C6 H10OH

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15
Q

Other types of sugars

A

Pentode monosaccharides are all the RNA ones and deoxyribose in dna and rna

Here glucose + glucose = maltose second sweet
Glucose + lactose = galactose last sweet after glucose
Glucose + fructose = sucrose which is sweetest

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16
Q

How toe join

A

When two alpha glucose molecule side by side oh groups interact under cindenssyion reactions, water lost but a covalent bond formed , this is a 1-4 glycosidic bond

This forms basis for joining together of glucos to make other polysaccharides like starch, which is amylopectin or amylose

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17
Q

Okay so first amylose of starch

A

1-4 glycosidic bonds
Twists into a helix which is further stabilised by hydrogen bonding
- this makes it further compact and much less soluble which is needed as this won’t affect the water potential gradient and thus it can be sued for efficient sotsgr of energy

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18
Q

Starch again

A

So joined by long chains of alpha helix under 1-4 glycosidic bonds
Twists to form a helix which makes it more compact snd ideal for staorsge
Also more insoluble and does not create a water gradient , so osmosis doesn’t enter water
Metabolically inactive . Good for storage

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19
Q

Amy,pectin second structure

A

Here again alpha glucose long chains under 1-4 glycosidic bonds but
Also some 1-6 glycosidic bonds , giving ranches to amylopectin
This happens every 1 in 25 times

The use of this is that more branches means more free ends for enzymes to catksyde hydrolysis reactions (adding of water to rbeak bonds) and release glucose

Also helix still and this makes more compact

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20
Q

So properties amylopectin sgsin

A

So branching one every 25 makes it more compact too so ideal for storage
- branched means more free ends so more enzymes can act in smoky or tin at once to ADD AND REMOVE GLUCOSE BOTH ACTUSKLY
# FINALLY still insoluble and doesn’t affect water potential gradient whereas before glucose did

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21
Q

Okay so what for animals

Why being more compact etc important

A

Amlupose and amylopectin was for starch and this is to store energy made from assimilated in ohtosytnedid

For animals it is glycogen
- Escaut same
- alpha glucose long chain with 1-4 glycosidic binding
- against eistd to fork helix and more compact, also insoluble
Inky difference is 1-6 glycosidic branching happens way mkreoftrnt, meaning more compact, and even more free ends

THIS IS IMPORTSMT BECAUDE animals are mobile so need better storage

Thus again more bshcnhigh makes it more easily hydroksied and so better efficacy , more compact and insolubke !

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22
Q

Hydrolsyisnis

A

Hydrolysis revatuodn opposite to condensation, adding water to break covalent bond and this is cslstdyed by enzymes

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23
Q

Last one? Cellulose

A

Cellulose this time not made by alpha gkucose
This one made by beta glucose
However as the hydroxyl groups on 1 and 4 are too far, in irder to fix this they are FLIPEPD UPSIDE DOWJ (not rotated ! But reflected)

Then a 1-4 glycosidic bond is still made, but every alternate beta glucose moneimer must be flipped for this to happen

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24
Q

What is the result if this

A

As a result the bond angle which is normally created doed not happen, meaning they cannot foul to form helix’s or branching cannot occur. This forms STRAIGHT CHAINS of brat glucose instead dwhich is useful for the file it okays in structure and support t

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25
Q

Cellulose is thus

A

King UNBRANCHED chains of beta glucose miners
Forming a straight chain that cannot coil
Now

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26
Q

Formation of cellulsoe form fibres

A

The beta gkucose monomers make long straight chains . MULTIPLE STSIGHT CHAINS THRN FORM HYDROGEN BONDS WITH ESCH OTHER TO FORM MICROFIBRILS

These then join to make macrifibrils
Which join to make whole cellulose fibres

Many microfibrils joine together to produce whole fibres
And di

Mic

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27
Q

Function of cellulose and why do we need

A

Well the hydrogen bonding between cellulose molecule old to form microfibrils gives it Zstrngth and keeps insolibke which is needed for cell walls

We need cellulsoe fibres as they provide the roughage needed for a good diet

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28
Q

Function key of dtrsgch or glycogen

A

This is the main energy store in animals and plants, and it converts soluble gkucose into insoluble polyssschirdes that are rfficneit for storage and can be hydrokysided when needed

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29
Q

But what I’d the key function of cellulose?

A

Instead if energy store, more if a physical role in protection and structure and god our digestive dydtem

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30
Q

Other functions of glucose?

A

Energ store, repsorstjoj , converted into sucrose in plants for transport as this id metbsokicslly kedd active, combined with edtrinsic lipids to make glycolipids and sued as antigens !

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31
Q

So finally summary

A

Amylose starch
= alpha 1-4 long chsins that coil and make helix good for strosge with hydrogen bonds but also insoluble
- amylopectin
- same thing but 1 in 25 is 1-6 glycosidic too forming branches, which more compact and more free ends so easily hydroksied
Glycogen for animals
Even more branching than amylopectin still insoluble and easily hydroksied and helix still formed

Cellulose
Beta this time where every other. Beta unit fluoped so that 1-4 glysocidc bonds till made e
But this makes stringer chains and so no could or branch
Multiple form hydrogen bonds to make microfibrils gives strength and insoluble
Microfibrils join make microfibrils join make oikyjer cellulose fibres lol

Structure rilem

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32
Q

All tests

A

Benedictus test for reducing and no. Reducing sugars

Biuert tedt for proteins

Iodine tedt for starch

Lipid emulsion tedt

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33
Q

What sugars are reducing and non reducing

A

Reducing = ALL MONOSACCHARIDES and some dissacrides = maltose and lactose

That means sucrose

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34
Q

you use bennedicts solution for reducing etc what is this

A

An alkaline solution of copper (2) sulfate

This can be propersred from

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35
Q

Benedict

A

Put sample in boiling , add equal amount of bennediftd in

  • boil forn2-5 mind until 70 or boil
  • if positive it goes from green yellow orange brick red predicate

If negative it stays blue, but it could still be non reducing

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36
Q

What happens

To make quantified?

A

Redcuijt sugars will react with copper 2 + ions and reduce to copper 1+ ions which are BRICK red

The higher the conc, the more copper 2+ ions will have reduced, and it is the amount of it that makes a different colour (less red = green, more red = orange , depending in the concentration

1) filter out the boiling tube to get rid of red private this leaves with you just blue
The more conc it was, more red will ahve left , leaving lighter blue
To get value, use a colorimeter
Here put sample in civette , then use distilled water as a control so it can be compared gains thst, put civette in and run a wavelength THAT IS OPPSITE COLOUR , here it is a red wavelength (630 nm wavlen5h (higher = red remember)
- then eithercheck for absorbs new or trnsmittsnce and compare against own or already made database

Alternative is to filter out the predicate, let it COMPLETELY DRY , and then weight them . The more preifoste = more cojdentrtsed

37
Q

Make own graph to find answers?

A

To do this need to serial dilution first

Alresydnplotngrsoh eith known concentrations based on their transmits cells or absorb acne scale, then use same growth tinfind use , do Benedictus tedt in each and plot concentration etc
You do abroance against concentration because you mesudring that

38
Q

Serial dilution?

A

Label tedt tube of each dilution
Forum fist full concentration add 1c,3 to other beaker and fill with 9cm3 distilled water

Do this again, remove 1 cm3 from their intonnect and fill

Keep doing this to the end by fsvotsof ten

Final one you can remove so that volumes all the same by 1c,3

39
Q

With non reducing sugars why don’t they work and how to do these

A

They have special link which doesn’t let them reduce so must density oink

So first 1) mix hydrochlriic acid with sample and boil in water carefully as acid dangerous
2. Then once finished neutralise with sodium hydrogen carbonate
Now bond broken can do Benedictus test completely again by boikign Benedictus solution and looking for colour

Remember if there positive tedt now = non reducing

Here = yellow orange brick red pricpstedagin!

40
Q

Bierutestedt?

A

Also an alkaline solution if copper 2 sulfate

Add birurest in and if this turns proteins (due to presence of PEPTIDE bonds) it is a protein

But if it stays blue it IS NIT

Hard way =

  • add solution to test
  • same amount of 10% NaOh
  • and drop by drop copper sukfste until it changes to BLUE
  • then give it 5 minutes to change colour to purple

Again

In presence of peptide bonds
Add = 10% an oh
Then drop by drop cusor3 until blue
Then wait 5 min

41
Q

Iodine test

A

First you need a solution cintsining iodine , so POTSDDIUM IODIDE aqueous

Add to sample, if it goes from orange brown to blue black = iodine roe sent , if it stays orange = no

Here plants you furdt need to boil to kill, add alcohol to remove chlorophyll and then do the tedt, this endured no ohoto happen and tedt Scutari. Can minsipltr conditions to show something is needed for ohotodythendts. For example but strip on leaf, destarch it for a day , and then boil kill ethanol do tedt if present only that’s ection remains irange yellown

42
Q

Emulsionntest for lipids

A

1) lipids and water don’t mix but adding ethanol will cause an emulsification with it
2) so add ethanol into mixture cintisnign lipids
3) and pour into ICE COLD WATER
4) if positive a white milky emus,ion forks

Shake it with

Remember for rest colorimetric time reset each toke and draw a calibration curve

More lipids= more jtkifbsle
Iodine in ootsdiuknidoieem

43
Q

How do biosensors work

A 
It is a device that uses BIOLGICAL molecule to detect a change 
These can be:
- a single strand of DNA 
- an enzyme 
- an antibody 
Will be on the strip

-
2) then in the presence of the sample, a reaction will happen, which will cause a change which a transducer picks up and CNVERTS INTO AN ELECTRICAL SIGNAL which then a database can check and produce a result

These molecule give specific reactions such as a base , a substrate or anti gene from antibody and this change is picked up

44
Q

How does a signal happen

A

Chemical change like change in oh or oxidation will cause a change in current that it can detect

Can be a number of ways such as enzymes that ctakyse into something else which is detected, more there was I first place of doemthing else and more change is

45
Q

Chromatographs

A

Ratio of how far thing dissolved into mobile phase comaoref to stationary m this is a vagueness

Carry out by putting pencil line and ink on the line sinit doesn’t dissolve snd tedt ruined
Bung on top so mobile phase done evslirstell

Talc is thin layer chromatography wotu a silica lsyer on plastic inert strip

46
Q

Why is talc good or bad than paper

A
  • cheaper to carry out and identify
  • however paper csnt form bonds with everything so talc more study can , such as acids
  • gives more specific separation of points do you can compare two chemicals in the SAME STRIP

Can be used with warmer temps which travels faster paper can’t
But expensive

47
Q

What are lipids made from

A

Carbon hydrogen and oxygen but MUCH LESS PROPRTION OF OXYGEN THEN CARBOHYDRSTES

Zlipids aremacromolecules = this means theybarenot built from repeating units like monomers

48
Q

Arenlipids polar

A

NO even thinhave polar hydrocyke regions they are not ss charge is spread out

So if nit polar can’t dissolve in water either !

49
Q

What are triglycerides

A

Trilhyceridesnisn a typemof lipid that is made from a glycoproteins and three fatty acids , where glycerol is a member of a group of kocleuos called alcohols , and fatty acid form csrbicykuc scid

They are bonded by the glycerol which is just propane with three alcohols and the carboxyl acid part of the fatty acid in Zcondesnation reactions called ESTERIFICATION , which forms ester covalent binds and three waters

To reverse this three water molecules must be supplied in hydrolysis , and enzymes ctakayse this
,
Ester bond is coooc

50
Q

Saturated vs unsaturated?

A

Saturated is without at least one carbon carbon double or triple bond

If they unsaturated the double bond causes the molecules to KINK/ BEND in their structure

The result of this id they cannot pack as closely tigether and London forces made are not as strictness

Thus they have lower melting and boiking points and instead are LIQUIDS AT ROOM TRKOERSTUREN

Thus they are described as oils instead of fats and this is common in plants

51
Q

Difference between okant and animal fats

A

Plants are liquid at room temp compare to animals as they are unsaturated , called OILS and apparently ire hwkthy , but any type of fat inebxcesd lesd to heart disease

52
Q

Phosphoipdsn

A

Modified triglyceride , still have glycerol but one fatty acid tail is replaced with a PO43- phosphate group

These have ohosphirs with Cabrini sdnnhdyrigennsnd oxygen and remember the oxygen is the one in low proportion.

53
Q

Properties of phosholipid

A

As phosphate groupnis charged, they are ALSO soluble in water, and so are hydrophilic
This is the reason they used in membrane

However due to their length the fatty acid tsils also are NON POLAR and don’t dissolve in water and so are hydrophobic

Thus charged head orient instead itself such that they are in othsidide with fatty acid tails in inside which remain interesting with themselves

This is called being a surface agent or a surfactant

Can thus interact with both aweuosinteriors and exteriors

54
Q

What are sterols

A

Another type of lipid odometer as steriod alcohols

Complex alohcol structure and has a 4 carbon ring structure with a hydroxyl group of the alcohol functional group st the end

This way they are both polar st this end and hydrophobic and non poslr through the 4 carbon ring structure

Thus they can interact in bilateral between hesd and tail

Here

55
Q

Cholesterol?

A

Body makes in liver and intestines , and plays function in cell membranes (regulating fluidity )
- here the Oh group interacts with the phosphate head and carbon ring with the tails, MIANLY BINDS TO THE TAILS, but interacts with hesds

This regulates fludity, it keeps the, not too close under low temps and cartelising , but also not too far apart and become fully liquid in high temps

Also makes more ridge by fircing to pack a bit closely but regulated thid

56
Q

Why do lipids being insolubke matter

A

Doesn’t allow water to go into cells in the blister key feature , and as.l lipids which are triglycerides , phospholipd and cholesterols are all insolubke !

57
Q

Cholesterol molduels

A

Vitamin d , steroid hormones and bile

58
Q

Key roles of lipids

A
  • in membranes ad phospholipids AND IN VESICLES , which can fuse
  • as a potential energy source in respiration
  • as a source of water in animals like camels who produce lipids to make water ( after condensation)
  • hormone production
  • INSULATION for animals like blubber , and also ELECTRICAL insulation for nerve transmission
    Waterproofing inn birds festherdetfb
  • ## CUSHIONING OF VITAL ORGSNS
59
Q

Lipids as an energy store?

A

Produce more energy in average, but the cinverdiond to get it takes a lot of energy too snd overall harder
- insoluble like starch and glycogen etc stoneojt affect water potential of cell components
- can hsve better storage such that more energy per unit but harder to edtrsft
# if staursted means more can be stored
And how used for respiration = hydrolysis where glycerol and fatty can acid use spesrslry

So that was
- more nerdy per unit but hsrd to extract
- iniosuble in water
- can be hydrokyside for products of respiration
-

60
Q

All amino acids have in common

A

Amine group - cHR - cOOH

R group is variable

61
Q

Amino acid joins when and what enzymes

A

It joins when the end of one NH2 group joins with the start of another COOH , losing water making a CONH PEPTIDE BOND !! This is condensation reaction and also broken by hydroksiso
When many amino acids join together by peptide bond they make a POLYPEPTIDE , this is csltysed by peptidoglycan transfersden

Then the r groups interact in 4 different ways kesding to different structures etc

62
Q

Sequence shape

A

Shape of a protein is determined by the sequence if the amino acids and the. R group interaction in different structures

63
Q

Descobee primary structure

A

Primarrybdteuctur described the linear sequence of amino acids in the sequence

This is determined by the bases sequence on the original section of dns mrna sss transcribed Fromm

This will determine the next

64
Q

Secondary structure if a protein

A

This is intisl folding of the protein due to hydrogen bonding between OXYGEN ATOMS OF CSBROXYLIC ACID GROUP SND THE HYDROGENS connected to hydrogen of amine groups. THIS IS DETERMINED BY THE PRIMSRY STEUFTURE, LINESR SEWUENCY OF AMINO ACIDS FIRST

SO secondary structure is the initial folding of protein due to hydrogen bond intervention beteeen atoms of polypeptide , determined by the amino acid sewuency of primary structure first

This csuses the protein to fold into either an ALPHA HELIX , or a Beta pleated sheat

D

65
Q

Tertiary structure?

A

This is the further folding of the protein into its 3D shape, determined by the secondary steucture . This because depdijg on how secondsrybpulls certain rules groups closer ornfurther away from each other . As a redult beta pleated sheets become fibriud proteins here and alpha globular

It is a resukt of R Grouo interceptions . These can happen in 4 ways

  • ionic bonding
  • covalent DISULPHIDE bridges = thede srejudtnvovslnet bonddbetween sulfur stoms !!
  • hydrogen bonds
  • London’s forces / van Dee was= this is weak hydrophobic hydrohokic intersvriojen
66
Q

Quaternary steufture?

A

Port will final steufture for protein
- here it is the result from linking beteeen two or more indivusk polypeotides called subunits , and this dependent on these intervsruond between r groups from DIFFERENT polypeptides

Intervsruojensrenthe swke , and it can be different polypeptdies or one

Like harmoglobin hsd 4

67
Q

Hydrophilic

A

Hydrohokic r groups tend to be on the outside to make it solubke and hydrohokic in inside - you will explore case studies of proteins later

68
Q

Protein test snd breakdown

A

Bieurted tedt, = maount of NAOH with solutionnsnd and coper sukfste, in presence of peptide bond turns puroles

To remove peptide bonds you need PROTEASE ENZYME , CALAYSES RVERSE RESCRION INTI INDIVIUAK AMINO ACIDS AGAIN , and this again hdyrolsycis reaction

69
Q

Common functions of proteins

A
  • hormones
  • cell signalling - glycoproteins act as receptors and peptide hormones 8
  • contractile muscles
  • energy store
  • structure? Keratin and collagen

Transport = hadmoglobij
Defensive in antibodies!

70
Q

What types of proteins globular snd fibrous do we need to know

A

Globulsr =

  • haemoglobin
  • insulin
  • catalase

Fibrous

  • keratin
  • elastin
  • collagen
71
Q

Basic knowledge of globular gs fibrous

A

Globular proteins = have function to either do with metabolism or functions in the body like signalling trsnsoort etc, whereas fibrous = structural and strength

Globular tend to be spherical with r groups on outside hydrohdyoicn and byydrphibic on inside, FIBROUS have. A higher promotion of hydrohokic r groups makijtnit insoluble

Globular normally spherical in shsoen
- and more variety of r groups , that dintrepeat and are more fomoledttoon, compared to a limited range which are simple and often reoestn

72
Q

Haemoglbij first
Function

Why is it easier to bind to an oxygen modules after it has alresdy bounded/ detached from one alreaydn?

A

Quaternary protein that is CONJUGATED ! This means it has a non protein component called a prosthetic group

Function = hamellgovin has to be able to bind with oxygen REVERSIBLY so it can carry it around the body from lungs and to cells snd vice verbs too

reversible means that it can both bind but also detach. Here every time it binds, it changes shape which makes it easier to bind to the next oxygen, and also when it detached same thing hsppend too

73
Q

Now steufture of harmoglboin

A
  • made from 4 polypeptide chains = 2 alphas and 2 beta subunits
  • each subunit contains a prosthetic haem Group, and this contains the ion IRON , which allows an oxygen molecule to bond . As a result each haemoglobin molecule can. Hind ti 4 oxygen molecules at one time
74
Q

Need to do key features globulsr vs fibrous

A
75
Q

Function of catalase

A

In metabolic resvtions and the liver body produces hydrogen peroxide as a by product, which is toxic, but catalase managed to catslyse the reaction of thid into water and oxygen which prevents and SMSed cells from OXIDIDATIVE DAMSGE !keepin safe

76
Q

Steufture catalyse “

What is catalase properties

A

This is sgsin 4 polypeptide chains and these all contain haem prosthetic group with iron ion sgsin

And the fsft that it has a prosthetic group like that allows the caltsdystions to happen

Cstlsse is an enzyme and being a biliguvsl catalyst it speeds up reactions without being used up itself

77
Q

Finally insulin globulsr function and prop tied

A

It is a hormone involved in regulation of BLOOD GLUCOSE LEVELS, if these are too high they are secreted at the liver which converts excess sugar into glycogen reducing sugar levels here and in muscles too

As it is a hormone it needs to be soluble so it can travel through blood, this is why gkibusle , and as it is hormone it must be a specific shsoenor it can’t work!

They are produced by beta cells in pancreas

78
Q

Structure of insulin

A
  • two polypeptide chsind , an A chain and B chains
  • A chain has 21 amino acids and B chain 30
  • here there are a few DISULPHIDE bridges between A chain and three for both
79
Q

Fibrous proteins properties

A

Repeated simple and not variety of r grouod gived orgsnsied structured whichnsingitsl for the roles fibrous proteins play in steufture

They tend to make loignsjdnstrijgnmoelcueks which don’t tend to fold into complex 3d structured like globular

They also unresctivein this sense

80
Q

Function of collagen

A
  • a connective tissue found in tendons ligaments and nervous system that acts as supporting structures giving strength and some elasticity cells
81
Q

Structure of collagen ?

A
  • three polypeptide chains that wound together in a triple helix rope like structure = gives it strength
  • many polypeptide chains form hydrogen bonds which makes staggered ends
  • this allows them to join need to end forming fibrils called tropocolagen
  • these then cross link to produce string fibres

So three polypeptide chain wounded in triple helix to form rope like structure
- hydrogen bonds form cause staggered ends which allows them to join need to end and form tropocoollagen fibrils which cross link to make even stronger
H bonds give staggered ends which allows tropcolalgen fibrils to form where cross links happen and better

82
Q

Collagen

A

I’d long and flexible under stress insoluble stuff and string

83
Q

Keratin function

A

Preeent in hair nails and skin with rolde of preventing tear snd scratched , structural snd protective function reducing damage to thede

84
Q

Structure + how is it varied

A

Has a large proprtion of cysteine r grouos which contain sukfur, this leads to MANY DISULFIDE BRIDGES and this gives strength

  • however more disuflide bridge the more string BUT LESS FLEXIBILE , nails have more , hair has less BUT MORE FLEDIBILE

THE NIRE FKEDIBILE THE LESS DISULFIDE BRIGE

85
Q

Elastin function

A

Elastin is present in like arterial walls and alveolus which allows them to expand when needed to continue pressure and cintrsct to original size , so provides elssricity even skin to return if pinched

86
Q

Elastin structure

A

Made from,any stretchy molecules called tropoelastin, which aggregate amongst hydrophobic regions , and then form cross links between r groups giving it strnegth but also keelign flexibility

87
Q

Summary fibrous euro toe is.

A

Collagen =
- 3 polypeptide chain tightly sounded triple helix rope like structure which gives strength
- hydrogen bonds for, give rise to staggered ends which alloe end to end joining, and this gives fibrils called tropcollagen which then cross link to give more stem eight
X collagen acts as connective tissue giving strength and elasticity to joints tendons ligaments nervous etc

Keratin is roles of sturcture and protection. To things like skin hair and nails which prevents damage like screaming
- high promotion of r groups cysteine which contains duo fur so many DISULFIDE bridges formed, yet the degree of this determines flexibility, more = less and this is shown in nails

Elastin allows for elasticity in things like alveoli and arteries walls so can expand but contract back to original shape

Has smash stretchy proteins molecule called tropoelstin which segregated smingst hydrohbpic regions. Then cross links from between to give it strength whilst also being elsdtic

88
Q

Final difference between glibular and firbouse

A

Sokuble DV’s insoluble
- complex r groups wider range and non repeating lnfromd more complex 3D shapes whereas fibrous have shorter repesting and less variety which leads to organised structure
- glibukarchsnged shape and is resctivesndnfibroud don’t change shape and unresvrige
# bodily functions whereas support and structure
- alpha helix vs beta pleated sheet
s

Bio Rev (12 decks)

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