BI L GIC!L " LEC#LES $E%ISI & S#""!$' "!

P
Example
Monomer (with formula)

Carbohydrate Starch/Glycogen

Cellulose

Lipid Fat / Phospholipid

!att" aci s # gl"cerol (# $hos$hate for $hos$holi$i )

Collagen

Protein Haemoglobin
* an * chains of 14+ an 14, a.a. each

%mino aci s (&l" ' () where ' an ( are leucine, isoleucine, $roline, h" ro)"$roline, h" ro)"line

(C1 OH below ring; C4 OH below ring; if above, the sugar is galactose)

C1 OH above ring (arrow). Note ifference between an glucose

Covalent -on 2ha$e of molecule

(1,4) gl"cosi ic . am"lose (1,4) an (1,,) . %m"lo$ectin an gl"cogen %m"lose3 Helical %m"lo$ectin3 -ranche helical &l"cogen3 branche helical H" rogen bon s between glucose resi ues of the same molecule, 1,4 gl"cosi ic bon creates helical com$act molecule

(1,4) gl"cosi ic

/ster lin0age

1e$ti e bon ;

1e$ti e -on , isul$hi e bon s &lobular $rotein Calle the globin fol

4inear with h" rogen bon cross lin0s between chains

4inear with 5hea 6 an three 5tails67 $olar hea an two non$olar tails for $hos$holi$i 9an er :aal6s interactions with surroun ing li$i 7$hos$holi$i molecules

!ibrous, tri$le helical bun les

-on s stabili8ing sha$e

H" rogen bon s between linear chains of cellulose, forming cross lin0s

!unction

2torage of energ" in $lant an animals

2tructural com$onent of cell wall

2torage of energ", com$onent of cell membranes

1o 1e$ti e bon between amino aci resi ues *o H" rogen bon s between gl"cine an ' ( of other * chains 4o 2mall si8e of gl"cine ensures closer $ro)imit" for better networ0 of h" rogen bon s to form fibrous tri$le heli) 2tructural su$$ort to muscle, ligaments

1+ ; $e$ti e bon *+ . numerous helices each stabili8e b" h" rogen bon s <+ ; 9=: interactions; h" rogen bon s, ionic interactions, each chain ative bon e to heme 4+ bin ing site of haeme stabili8e b" ative bon ing with His; <= sha$e b" h" ro$hobic interactions >rans$ort of o)"gen to ifferent organs of the bo "

2"nthesise b" 2olubilit" in water

Chloro$last in $lant cells, &olgi in animal

&olgi a$$aratus

2mooth /?

?ibosomes7?/?

?ibosomes ?/? of cells in bone marrow 2oluble

@nsoluble

@nsoluble

@nsoluble

@nsoluble

(16) glycosidic

=iagram

(14) glycosidic

"acromolecule
2tarch

Structure
1. *. <. 4. Contains am"lose an am"lo$ectin am"lose contains 1+++ A glucose resi ues lin0e b" 1,4 lin0age am"lo$ectin contains over 1,+++,+++ A glucose lin0e b" 1,4 an 1,, lin0ages Helical sha$e with h" rogen bon s forming between ever" ,th glucose H;bon s face core of heli).

$elating to(
1. am"lose an am"lo$ectin have A lin0ages which can easil" be bro0en b" am"lase to release large amounts of glucose ver" Cuic0l".

Function
2torage of glucose in $lant cells.

4. B. &l"cogen Cellulose B.

Helical sha$e ma0es the molecule com$act, allowing large amounts to be store in cells. no grou$s are available to form H;bon s with water, ma0ing starch an gl"cogen insoluble 2torage of glucose in animal cells 2tructural su$$ort in cell walls.

>rigl"ceri e 1hos$holi$i

2imilar to am"lo$ectin but greater branching (more 1,, lin0ages) 1. Numerous chains of D glucose lin0e b" D (1,4) gl"cosi ic *. /ver" alternate glucose resi ue is inverte <. 4inear molecule with e)tensive cross lin0ing with other cellulose molecules 1. >hree fatt" aci s covalentl" bon e to gl"cerol b" ester lin0age 1. *. >wo fatt" aci s an $hos$hate grou$ Eoine b" ester lin0age !att" aci chain length an saturation of h" rocarbons var" >ri$le heli) each consisting of re$eating &l";';( 4inear re$eating units /)tensive cross lin0ing between chains Contains two an two D chains of 14+ an 14, aa res$ectivel" hel in a globin fol /ach chain contains man" al$ha helices each chain contains a heme grou$ ($or$h"rin ring # !e ion) 4. 1or$h"rin ring is ative bon e to Fth a.a. histi ine on the rings

2imilar to starch 1. *. <. 1. 1. 2. D gl"cosi ic lin0age has less rotational free om than A lin0age ma0ing the structure of cellulose linear %llows for e)tensive cross lin0ing with neighbouring chains resulting in high tensile strength for cellulose ga$s between the cross lin0s allow water an other solutes to $ass through ma0ing cellulose $ermeable. >rigl"ceri es are non;$olar, with high $ro$ortion of h" rogen to carbon an o)"gen. am$hi$athic (h" ro$hobic tails an h" ro$hilic hea s) Chain length an egree of saturation affect flui it" of $hos$holi$i s (refer to membrane !lui mosaic mo el) %llows for closer interaction of three chains, resulting in e)tensive H;bon formation between ' of *n chain an ( of thir . &ives regular fibrous sha$e to collagen % s to stabilit" of tri$le heli) an ma0es it rigi globin fol globular $rotein, ma0es the $rotein soluble in water allowing haemoglobin to issolve in the c"to$lasm of the ?-C 2econ ar" structure contributes to stabilit" of tertiar" structure Heme grou$ bin s reversibl" to o)"gen (-ohr /ffect) an trans$orts o)"gen from lungs7gills to tissues /nsures stabilit" of ring an allows for coo$erative effect where the o)i ation of one !e#* causes the accelerate o)i ation of the other !e ions in the molecule

2torage of energ" an metabolic water; -uo"anc" an electrical7thermal insulation 1. %cts as selective barrier in cell surface membranes. *. Membrane flui it" can be increase b" higher unsaturation an shorter h" rocarbon chain length 2tructural su$$ort of animal tissue s0in, cartilage, ligaments etc.

Collagen

1. *. <.

1. *. <. 1. *. <. 4.

Haemoglobin

1.
*. <. 4.

1. >rans$ort of o)"gen from lungs to tissues