All About Protein

7/25/2019 All About Protein

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RUZANNA BT AHMAD SHAPII(158983)

NOR DALILA BT HASHIM (156293)

EPF 4602BIOMATERIAL POLYMER

TEHNOLO!Y


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WHAT IS PROTEIN?

P"#$%&' is a large biologicalmolecule consisting of one or morechains of amino acids.


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STRUTURE OF PROTEINLINEAR

STRUTURE

&'%" ""'*%+%'$ #, +&'# -&./ L&'%. -#%'$ &'*%/ /- /

.&/.% #'./ %$7%%' +&'# -&./

SEONDARYSTRUTURE

,#.&'* #" -#&&'* 7&$&' "#$%&':%;+%/ &'-.% %&-%/ '.%$%. /%%$/

/$&&UARTENARYSTRUTURE

&'. +$&% #%$&.%/ &'$# /&'*%? "*%" "#$%&'

H%+#*#&' / @$%"'" /$"-$"%.% $# //#-&$' #, $7# *#&' '. $7# %$ *#&'

#"#$%&'/


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STRUTURE OF PROTEIN


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LASSIFIATIO

N OF PROTEIN


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Simple proteins

chains of amino acid units only joined by peptide

linkages. Examples are : Egg albumin,

serum globulins, glutenin inwheat, coryzenin in rice,

tissue globulin, etc.

Conjugated proteins

composed of simpleproteins and non proteinmaterial.

The non-protein material iscalled prosthetic group orcofactor

Examples are ucin insali!a "prosthetic group,carbohydrate#, casein inmilk "prosthetic group,phosphoric acid#,haemoglobin in blood"prosthetic group, ironpigment#, etc.


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S&+% P"#$%&'


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#'*$%. P"#$%&'


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madeupofpolypeptidechainsthatrunparalleltotheaxisheldtogetherbystronghydrogenanddisulphidebondscanbestretchedandcontractedlikeathreadusuallyinsolubleinwater.Examplesare:a-keratin"hair,wool,silkandnails#$myosin

"muscles#$collagen"tendons,bones#,etc.

%ibrousproteins

ha!emoreorlesssphericalshape"compactstructure#a-helicsaretightlyheldupbyweakattracti!eforcesof

!arioustypes:&ydrogenbonding,disulphidebridges,saltorionicbridges.

usuallysolubleinwater.Examplesare:'nsulin,pepsin,haemoglobin,cytochromes,

albumins,etc.

(lobularproteins


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PHYSIAL

PROPERTIES OFPROTEIN


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SIZE AND SHAPE Si!e of "rotein usuall# measured in molecular

$eight %mass&. 'olecular $eight of "rotein is the mass of one

mole of "rotein usuall# measured in units

daltons. It can be estimated b# methods including

electro"horesis( gel )ltration( and more

recentl# b# mass s"ectrometr#.

'ost "roteins ha*e a mass bet$een +, and

+,, -ilodaltons %-&.

A small "rotein consists of about /, amino

acids $hile larger "roteins ma# contain 0(,,,


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HYDROPHOBIITY

H#dro"hobic means fear of $ater. In a1ueous solutions( "roteins tend to fold

so that areas of the "rotein $ith

h#dro"hobic regions are located in internalsurfaces ne2t to each other and a$a# from

the "olar $ater molecules of the solution.


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Polar grou"s on the amino acid are

called h#dro"hilic %$ater lo*ing&because the# $ill form h#drogen

bonds $ith $ater molecules.

The number( t#"e and distribution ofnon"olar amino acid residues $ithin

the "rotein determines its

h#dro"hobic character.


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SOLUBILITY Solubilit# is the amount of a solute that

can be dissol*ed in a sol*ent. The 03 structure of a "rotein a4ects its

solubilit# "ro"erties.

5or e2am"le6#to"lasmic "roteins ha*e mostl#h#dro"hilic %"olar& amino acids on theirsurface and are therefore $ater soluble(

$ith more h#dro"hobic grou"s located onthe interior of the "rotein( sheltered fromthe a1ueous en*ironment.


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In contrast( "roteins that reside in the li"id

en*ironment of the cell membrane ha*e mostl#h#dro"hobic amino acids %non "olar& on their

e2terior surface and are not readil# soluble in

a1ueous solutions.

An# changes to condition such as bu4er( sol*ent

t#"e( "H( ionic strength and tem"erature $ill

cause "rotein to lose the solubilit#.


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ISOELETRI POINT

The isoelectric point %"I& of a "roteinis the "H $here the net charge onthe "rotein is !ero.

Proteins ha*e di4erent isoelectric"oints because of their di4erentamino acid se1uences.

The# can be se"arated b# ad7ustingthe "H of a solution.


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APPLIATION

OF PROTEIN


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FOOD INDUSTRY

!%&'* *%'$

3 8i*e sha"e and structure to food.

E+/&%"/

3 Emulsions in food are mi2tures of oil and

$ater.

3 'a#onnaise contains oil and $ater. The

emulsi)er -ee"s these mi2ed and$ithout it

the oil and $ater se"arate.


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F#+&'* *%'$

3 'aterial that facilitates formation offoam.

T&-%'%"/

3 Thic-ening agents ma-e foodsthic-er.


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RYSTALIZATION

To form a high31ualit# cr#stal( a"rotein must be immobili!ed in alattice in a consistent conformation

$ith limited d#namic motion. Protein surface "ro"erties "la# a

determining role in controllingcr#stalli!ation beha*ior becauseformation of tight( geometricall#"recise intermolecular contacts isre1uired for lattice stabilit#.


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FABRI FROM ELASTIN Elastin is a matri2 "rotein. It holds the cells

together into tissues and "ro*ides naturalsu""ort and 9e2ibilit#.

It gi*es s-in and blood *essels their

elasticit#. Elastin $ill ser*e as a sca4old $hich can

be se$ed or glued in the "lace of amissing "art.

It $ill hold the arter# or organ closed andintact $hile at the same time it can alsobe "o"ulated b# the bod#:s o$n cells
http://www.nytimes.com/2005/06/21/science/21elas.html?_r=1&


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SOY PROTEIN=BASEDPLASTIS

lending so# "rotein $ith "ol#esters usinga "ol#*in#llactam as a com"atibili!ersuccessfull# made so# "rotein3based

"lastics. The blends $ere "rocessed b#

com"ounding e2trusion and in7ectionmolding.

lends made from so# "rotein 9our"roduced "lastics $ith the lo$est $aterabsor"tion.
http://link.springer.com/article/10.1023%2FA%3A1021018022824


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T' #

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