molecules smallbutimp vitamins3minerals
micro
n proteinscan be a source of energy H ÉÉo II I H E
I ans ch
smallestaminoacid glycine has H group Glycine alanine ca chs I
secondsmallestamino acids alanin leucine isoleucine proline valine m
n tryptophan methionine acarbons
glycinehas nochiral center 3 has no D or L polaramino acids
all aminoacids have a freecarboxylic acid 3 amino H É i o n Iti o
da
exceptof proline it is considered a secondaryamine H É on If
oil
s't
methane 3 cysetine the onlytwocontainingsulfur g cysteine
methane is inertbecause its in themiddle threonine Asparagine
gutamine C 6carbon
cysteine isterminal so its interacting 3 canformdisulfidegroup Acidic amino acids basic amino acids
aminoacids are buildingblocksofprotein o H ÉÉ o o m ite
gym tiff a
the Ich d CH
i
z N c th
n all aminoacids can work as abutler at both basic asparatate glutamate 4th
nth H
environment 3 at acidicenvironments y Histidine
pHof blood 7.3 7.4
pHof bloodtoacidosis pHofblood t alkanosis specificsequence ofaminoacidsthatare chterminds bygenes
if itsacidicyouaddH 3 basicyouremove theH n themostimp istheprimarystructure 3 is notfunctional it
N terminal on NH side c terminal on coo side determinesthefunction
mm theonly bondsfound intheprimarystructure arethepeptide
peptidebond is shorterthan a normalsinglebond 3 is bonds homolugus similarnotidentical
plannar it has doublebond characteristics its stronger a helix has3 consecutive amminoacidsper eachturn
thansinglebond 3 can't bedestroyedwithout an enzyme n hydrogenbond is weakbut agroupofhydrogenbonds arestrong
proteins can beusedas Atp butisn't its mainfunction u whenproline3glycine arethereit willdisruptthe L helix
n proteinscannotstoreamino acids
primarystructure is stabalized bypeptidebonds
prolens can beseparated into simpleproteins and secondarystructure is stabalizedbyhydrogenbonds
conjugatedproteins thatare attached to non proteins R groupor sidechainsstabalizesthetertiarystructure
, non polar aminoacid associated with the withoutchaperons we will have dillvent results
lipid bilayer onlyone will end up functional and therestwon't
if we replace an acidic a a with another among fibrousproteins he havekeratin 3 silk
acidic a a
nothing will change but if we replace fibers
a polar a a with a non polar it willchangethe n the silk fibers are made of 13 pleated sheets
structure and keratin is made up of L helix
not all proteins have a Quaternarystructure n keratin is Quaternary because its functional and
hemoglobin has Qutarnery and myoglobin has subunits
has tertiary structure n in myoglobin and hemoglobin we have twohistadie
Domains are found around the same that are extremelyimportant in theattachment of the
sequencethey have 1 N terminal 3 I c terminal hemoglobin tothe protein 3 stabalication of the
Subunits has morethan I domain hasmany oxygen with the heme
C 3 N terminals n myoglobin is a protein mainly found in
when the body tempgoes toohigh proteins will muscles and the purpose is to store oxygen 3
start todenature and lose their 3Dstructure its whatusuallygives themusch its redcolor
denature can never disturb proteinprimarystructure n
primaryfunction is to transport oxygen from
hydrolosis disturbs the proteinsprimarystructure the lungstothetissue
causesof denaturation in our biologicalstate its hemoglobin has twoforms
hightemperature 3 Strongacid or base T tout deoxygenated
foldedstructure is themostfunctional structure
3 R Relaxed oxygenated
fromtheenergy
whyis it thatwhen a proteingetsheated it doesn'tgoback n low PH is acidic
to its primaryfunctionalstate Bohor elliot is the elect of pH on allinity
toassurethat everytime we synthesize a protein in our X PH F acidity I allinity
body that it is properlyfolded 3 we have another M PH 41 acidity I allinity
M PH ve charge
N PH the charge
micro
n proteinscan be a source of energy H ÉÉo II I H E
I ans ch
smallestaminoacid glycine has H group Glycine alanine ca chs I
secondsmallestamino acids alanin leucine isoleucine proline valine m
n tryptophan methionine acarbons
glycinehas nochiral center 3 has no D or L polaramino acids
all aminoacids have a freecarboxylic acid 3 amino H É i o n Iti o
da
exceptof proline it is considered a secondaryamine H É on If
oil
s't
methane 3 cysetine the onlytwocontainingsulfur g cysteine
methane is inertbecause its in themiddle threonine Asparagine
gutamine C 6carbon
cysteine isterminal so its interacting 3 canformdisulfidegroup Acidic amino acids basic amino acids
aminoacids are buildingblocksofprotein o H ÉÉ o o m ite
gym tiff a
the Ich d CH
i
z N c th
n all aminoacids can work as abutler at both basic asparatate glutamate 4th
nth H
environment 3 at acidicenvironments y Histidine
pHof blood 7.3 7.4
pHof bloodtoacidosis pHofblood t alkanosis specificsequence ofaminoacidsthatare chterminds bygenes
if itsacidicyouaddH 3 basicyouremove theH n themostimp istheprimarystructure 3 is notfunctional it
N terminal on NH side c terminal on coo side determinesthefunction
mm theonly bondsfound intheprimarystructure arethepeptide
peptidebond is shorterthan a normalsinglebond 3 is bonds homolugus similarnotidentical
plannar it has doublebond characteristics its stronger a helix has3 consecutive amminoacidsper eachturn
thansinglebond 3 can't bedestroyedwithout an enzyme n hydrogenbond is weakbut agroupofhydrogenbonds arestrong
proteins can beusedas Atp butisn't its mainfunction u whenproline3glycine arethereit willdisruptthe L helix
n proteinscannotstoreamino acids
primarystructure is stabalized bypeptidebonds
prolens can beseparated into simpleproteins and secondarystructure is stabalizedbyhydrogenbonds
conjugatedproteins thatare attached to non proteins R groupor sidechainsstabalizesthetertiarystructure
, non polar aminoacid associated with the withoutchaperons we will have dillvent results
lipid bilayer onlyone will end up functional and therestwon't
if we replace an acidic a a with another among fibrousproteins he havekeratin 3 silk
acidic a a
nothing will change but if we replace fibers
a polar a a with a non polar it willchangethe n the silk fibers are made of 13 pleated sheets
structure and keratin is made up of L helix
not all proteins have a Quaternarystructure n keratin is Quaternary because its functional and
hemoglobin has Qutarnery and myoglobin has subunits
has tertiary structure n in myoglobin and hemoglobin we have twohistadie
Domains are found around the same that are extremelyimportant in theattachment of the
sequencethey have 1 N terminal 3 I c terminal hemoglobin tothe protein 3 stabalication of the
Subunits has morethan I domain hasmany oxygen with the heme
C 3 N terminals n myoglobin is a protein mainly found in
when the body tempgoes toohigh proteins will muscles and the purpose is to store oxygen 3
start todenature and lose their 3Dstructure its whatusuallygives themusch its redcolor
denature can never disturb proteinprimarystructure n
primaryfunction is to transport oxygen from
hydrolosis disturbs the proteinsprimarystructure the lungstothetissue
causesof denaturation in our biologicalstate its hemoglobin has twoforms
hightemperature 3 Strongacid or base T tout deoxygenated
foldedstructure is themostfunctional structure
3 R Relaxed oxygenated
fromtheenergy
whyis it thatwhen a proteingetsheated it doesn'tgoback n low PH is acidic
to its primaryfunctionalstate Bohor elliot is the elect of pH on allinity
toassurethat everytime we synthesize a protein in our X PH F acidity I allinity
body that it is properlyfolded 3 we have another M PH 41 acidity I allinity
M PH ve charge
N PH the charge
