Lecture 1
what
heh andstructuralcomplexity
extracttransformand
useenergyfromenvironment
ionsor organism'scomponentsandregulatedinteractionsamongthem
E senseandrespondto environment
life isbuiltbycomplexmacromolecules
lifeneedslargeorganicmolecules tofunction
withoutinputofenergy moleculesdecaytowards moredisorderedstatesandcometoequilibriumwithitssurroundingsandbreakintosmall
solifeneedscontinualinputofe fromenvironment
nergy
cellshaveplasmamembrane
I II Iportenergysourcesandrawmaterials
2 exportwaste
lipidmembraneservesas selectivebarrier
why to i allowtohavegreaterconcentrationsofnutrientsandsynthesizedproductsinsidecell
membranes
allowcellstohavea distinct
i11IT
adininia9iItriu'hiii Thihdings
acompositionofinsidecelli
roteinsaccomplishmostmolecularfunctions differentfromoutsidecel
eachproteinservesasa specificfunction
servestructuralroles
generatemovement
senseanddetectsignals
manyproteinscatalyzereactions enzymes
eneticinformationisstoredinDNA
selfreplicate isinDNA
chemically Dnaismuchsimplerthanproteins
iii iii am
20buildingblocks aminoacids
iii iii iii iii
makesproteins
iii in's in io.iiiimacnineca.caribosome
3 ribosomessynthesizeproteinsusingintoinRNA in cytoplasm
translation
cus init intine sie
directionofthisflow protein RNA
DNAisrequiredasatemplatetosynthesizeDNA
ansiationoccursby readingnucleotides in triplets noneedto memorize ch
ribosomes incorporatespecificaminoacidsusinggeneticcode
there's 4nucleotidesandsoaminoacids
ti greater
mail.in i a i i m'iiiin
2otherRNAsrequired in translation
tRNA coupledtoaminoacidresidue
pairswithmrnasequencetoconvertsequenceincodonsintospecific
aminoacids
ribosomesarecomposedofproteinsandribosomalRNA rrna
theplacewhereproteinsynthesishappenisinRNAmolecule
,lecture 2 Buildingblocksandmacromolecules
neoincellsincarriedby macromolecule
polype
RNA
proteins
mostcommontypeofpolyster
mon.in
stiiiiiiiiiiiiiiiiiiiiieromanesitpoiar
HowtocookPET requiresmixing aprecursors
1inputofenergyheat 150290C
aremovalofbyproducts likemethanol
tiae
me iii
have centralcarbonatom ca
aminogroup
carboxylgroup
peptia Ñ iesamino
acidsdiffer
aminoacidsarejointtogetherbycarboxylgroupinonebondedtoaminogroupoftheother resultsinpeptidebondforma
backbone ofproteinislinearchainofcarbonandnitrogenatoms
thatcontainpeptidebonds
sidegroupsstickoutof backbone
haveorientationwithaminogroupatoneendinterminusandcarboxylgroupatothercoterminus
startofprotein 3endofprotein
firstaahastreeNHZ blastaahastreecourt
sidechainsprovide chemical
i dentity to aminoacid
20differentsidechains 20diffaminoacids
humansandothermammalscansynthesize isaminoacids
arestareessentialaminoacids mustcomefromourdiet
Éit
e Eggnog
igemical
reactIT
iii ii
onlyspecialamino
3 groupsofaminoacids
meinwater
eithercontainlinearorbranchedhydrocarbons oraromaticrings
2 hydrophilic
verysolubleinwater
denuaration
either basic acidic orpolarwithunchargedgroups
itsspecial
reactivesulfhydrylgroupsie reasonwhy
serveincatalysisof enzymes
goodfor
s tructure ucanreactwithothercysteinestoformdisulfidebondstojoinapolypeptides
i Ih
forms
T.GE n.I enI I.gg
incorporation of
bondto
covalent
itleadstokinksinlinearchain
n inaminogroupattachedto a csigaraig.eet
Linearpolypeptidechainsfoldintospecific3Dstructuretohaveafunction
Y monomersisnucleotides
bbackbonephosphate iscomposedof pentose scarbonsugar
andacoT
ribose
group phosphate
group
baseringshaped
nitrogenous moleculecontainingnitrogen
negativechargeinphosphatemakesthemacidic
, haveribophosphatebackbone
joinedthroughaphosphodiestercovalentbonds
phosphategroup link a deoxyriboseat sand3
diffbasetohaveuniquesequence
it
haveorientation sendphosphatein'd Tamiya p gig
DNA vs RNA
ribonucleicacid is a deoxyribose
pentose deoxy pentoseribonucleicacid isribose
baifference
islossof on atposition 2 deoxyribose
Thyminebase base
hydrogenbondsweak
noncovalent
c hEner
qi9
doublestranded.com m
as3to s andothersto3 orientation
go.name
liEn bondsbetweenhydrogenbonds but
weaklycovalent sincethere'salotofbonds keeps astrands
together
bribophosphatebackboneoutside
baseinsidespaced osunmappart wideandhaveuniquechemicalinto
turnevery3.43.6mmco10sbasesperturn
complete two
on
outside spacebetweenstrandsformahelicalgrooveman aminor andcannotdistinguishallbases
shallow
atomsonedges
areexposed p
containpairoffusedrings
2typesof bases
containsinglering basesareconnectedtoribosethroughNatomat 9
p PYI.
2nAmoreproneto breakingthanDNA
hydroxylgroupatposition2 inribosecanspontaneouslyreactwithphosphategroup breakRNAmolecule
whyDNAismorestableandchoiceofgeneticmaterial
isitlacksonat a ribose
someviruseshavegenomesofrna longest groupis 40,000nucleotideslong
oneinNidovirales
DNAinourgenomearehundredsofmillions
ofbasepairscapinlengthConromosomes
structureofDNA proteinstoreadsequencewithoutunwindingdoublehelix
allowsDNAbinding
mostproteinDNAinteractionsusemajorgroove
him ami idstereoisomerstoformproteins
bbecauseitsmorebeneficial
ifwesynthesizeproteinshalfwillbe
useofsame20
amino andconservation ofcodonsthatcodeeachofthem
acids
fromhumantobacteriaproducesameprotein
movingagene
998 a
catalyticsiteofribosomesisinrrnasimilar
across
o rganisms
, ecture3 proteinstructure
proteinfunctionisdetermined
bytheirstructure
erarchyofproteinstructure
Iiii
nearpolypeptidechainsfoldintospecific3Dstructurestoacquireafunction
Trimarystructure sequence
hasdirectionality withbeginningavterminusandend cterminus
atomicmassunit
I in re it meroeaaresiduesandintheirmass in.at p
smallestproteinsare 40aa inlength
averageproteindependsonorganism Da
massof 1 aa 110
inyeast averageis466an residues
largestproteinhas34000aa residues
oligopeptides smallchains so
aa
iiieii ii
26akDa bluelightandtransformit
absorb intogreenlight
energy blue energy ox
secondary structure ight
coreefften
peptidechainbackbon.ms
arrangements ofaas
I
ocalconformationsof
generatestablearrangementsofanresidues stabilized
byrebonds
amajorpeptidechainbackbone
Il to basedon abondingbetweenpeptidebondcarbonyloatomsononeaminoandamidenatomsonotheraa res
makesup 60 oflengthofaveragepolypeptidechain
sureofoneaa atpositionin forms abondwithcoofsecondaaatposition na
stiltedaxisgeneratesperiodicityof3.6aa residuesturn
backbone hasstraightrodstructurewithsidechainspoinitingoutwards
surfacepropertiesdependonsidechains
prolineis notfoundahelix determinepropensity ofahelixformationanditsinteractionswithotherpartsofproteinand
molecules
E iii i
B sheets
short ssaal nearlyfullyextendedsegments
H bonds areformed between a ssheetsoriented tochainsofbackbone
alignmentof2ormoreastrandsmakenearly 2 dimensionalsheets
sidechains aboveand belowasheetplane
priggata
baetermine
interactionswithin
proteinandmoleculesandpropensitytoform
organization
insamepolypeptidecanbeparallelorantiparallel
what
heh andstructuralcomplexity
extracttransformand
useenergyfromenvironment
ionsor organism'scomponentsandregulatedinteractionsamongthem
E senseandrespondto environment
life isbuiltbycomplexmacromolecules
lifeneedslargeorganicmolecules tofunction
withoutinputofenergy moleculesdecaytowards moredisorderedstatesandcometoequilibriumwithitssurroundingsandbreakintosmall
solifeneedscontinualinputofe fromenvironment
nergy
cellshaveplasmamembrane
I II Iportenergysourcesandrawmaterials
2 exportwaste
lipidmembraneservesas selectivebarrier
why to i allowtohavegreaterconcentrationsofnutrientsandsynthesizedproductsinsidecell
membranes
allowcellstohavea distinct
i11IT
adininia9iItriu'hiii Thihdings
acompositionofinsidecelli
roteinsaccomplishmostmolecularfunctions differentfromoutsidecel
eachproteinservesasa specificfunction
servestructuralroles
generatemovement
senseanddetectsignals
manyproteinscatalyzereactions enzymes
eneticinformationisstoredinDNA
selfreplicate isinDNA
chemically Dnaismuchsimplerthanproteins
iii iii am
20buildingblocks aminoacids
iii iii iii iii
makesproteins
iii in's in io.iiiimacnineca.caribosome
3 ribosomessynthesizeproteinsusingintoinRNA in cytoplasm
translation
cus init intine sie
directionofthisflow protein RNA
DNAisrequiredasatemplatetosynthesizeDNA
ansiationoccursby readingnucleotides in triplets noneedto memorize ch
ribosomes incorporatespecificaminoacidsusinggeneticcode
there's 4nucleotidesandsoaminoacids
ti greater
mail.in i a i i m'iiiin
2otherRNAsrequired in translation
tRNA coupledtoaminoacidresidue
pairswithmrnasequencetoconvertsequenceincodonsintospecific
aminoacids
ribosomesarecomposedofproteinsandribosomalRNA rrna
theplacewhereproteinsynthesishappenisinRNAmolecule
,lecture 2 Buildingblocksandmacromolecules
neoincellsincarriedby macromolecule
polype
RNA
proteins
mostcommontypeofpolyster
mon.in
stiiiiiiiiiiiiiiiiiiiiieromanesitpoiar
HowtocookPET requiresmixing aprecursors
1inputofenergyheat 150290C
aremovalofbyproducts likemethanol
tiae
me iii
have centralcarbonatom ca
aminogroup
carboxylgroup
peptia Ñ iesamino
acidsdiffer
aminoacidsarejointtogetherbycarboxylgroupinonebondedtoaminogroupoftheother resultsinpeptidebondforma
backbone ofproteinislinearchainofcarbonandnitrogenatoms
thatcontainpeptidebonds
sidegroupsstickoutof backbone
haveorientationwithaminogroupatoneendinterminusandcarboxylgroupatothercoterminus
startofprotein 3endofprotein
firstaahastreeNHZ blastaahastreecourt
sidechainsprovide chemical
i dentity to aminoacid
20differentsidechains 20diffaminoacids
humansandothermammalscansynthesize isaminoacids
arestareessentialaminoacids mustcomefromourdiet
Éit
e Eggnog
igemical
reactIT
iii ii
onlyspecialamino
3 groupsofaminoacids
meinwater
eithercontainlinearorbranchedhydrocarbons oraromaticrings
2 hydrophilic
verysolubleinwater
denuaration
either basic acidic orpolarwithunchargedgroups
itsspecial
reactivesulfhydrylgroupsie reasonwhy
serveincatalysisof enzymes
goodfor
s tructure ucanreactwithothercysteinestoformdisulfidebondstojoinapolypeptides
i Ih
forms
T.GE n.I enI I.gg
incorporation of
bondto
covalent
itleadstokinksinlinearchain
n inaminogroupattachedto a csigaraig.eet
Linearpolypeptidechainsfoldintospecific3Dstructuretohaveafunction
Y monomersisnucleotides
bbackbonephosphate iscomposedof pentose scarbonsugar
andacoT
ribose
group phosphate
group
baseringshaped
nitrogenous moleculecontainingnitrogen
negativechargeinphosphatemakesthemacidic
, haveribophosphatebackbone
joinedthroughaphosphodiestercovalentbonds
phosphategroup link a deoxyriboseat sand3
diffbasetohaveuniquesequence
it
haveorientation sendphosphatein'd Tamiya p gig
DNA vs RNA
ribonucleicacid is a deoxyribose
pentose deoxy pentoseribonucleicacid isribose
baifference
islossof on atposition 2 deoxyribose
Thyminebase base
hydrogenbondsweak
noncovalent
c hEner
qi9
doublestranded.com m
as3to s andothersto3 orientation
go.name
liEn bondsbetweenhydrogenbonds but
weaklycovalent sincethere'salotofbonds keeps astrands
together
bribophosphatebackboneoutside
baseinsidespaced osunmappart wideandhaveuniquechemicalinto
turnevery3.43.6mmco10sbasesperturn
complete two
on
outside spacebetweenstrandsformahelicalgrooveman aminor andcannotdistinguishallbases
shallow
atomsonedges
areexposed p
containpairoffusedrings
2typesof bases
containsinglering basesareconnectedtoribosethroughNatomat 9
p PYI.
2nAmoreproneto breakingthanDNA
hydroxylgroupatposition2 inribosecanspontaneouslyreactwithphosphategroup breakRNAmolecule
whyDNAismorestableandchoiceofgeneticmaterial
isitlacksonat a ribose
someviruseshavegenomesofrna longest groupis 40,000nucleotideslong
oneinNidovirales
DNAinourgenomearehundredsofmillions
ofbasepairscapinlengthConromosomes
structureofDNA proteinstoreadsequencewithoutunwindingdoublehelix
allowsDNAbinding
mostproteinDNAinteractionsusemajorgroove
him ami idstereoisomerstoformproteins
bbecauseitsmorebeneficial
ifwesynthesizeproteinshalfwillbe
useofsame20
amino andconservation ofcodonsthatcodeeachofthem
acids
fromhumantobacteriaproducesameprotein
movingagene
998 a
catalyticsiteofribosomesisinrrnasimilar
across
o rganisms
, ecture3 proteinstructure
proteinfunctionisdetermined
bytheirstructure
erarchyofproteinstructure
Iiii
nearpolypeptidechainsfoldintospecific3Dstructurestoacquireafunction
Trimarystructure sequence
hasdirectionality withbeginningavterminusandend cterminus
atomicmassunit
I in re it meroeaaresiduesandintheirmass in.at p
smallestproteinsare 40aa inlength
averageproteindependsonorganism Da
massof 1 aa 110
inyeast averageis466an residues
largestproteinhas34000aa residues
oligopeptides smallchains so
aa
iiieii ii
26akDa bluelightandtransformit
absorb intogreenlight
energy blue energy ox
secondary structure ight
coreefften
peptidechainbackbon.ms
arrangements ofaas
I
ocalconformationsof
generatestablearrangementsofanresidues stabilized
byrebonds
amajorpeptidechainbackbone
Il to basedon abondingbetweenpeptidebondcarbonyloatomsononeaminoandamidenatomsonotheraa res
makesup 60 oflengthofaveragepolypeptidechain
sureofoneaa atpositionin forms abondwithcoofsecondaaatposition na
stiltedaxisgeneratesperiodicityof3.6aa residuesturn
backbone hasstraightrodstructurewithsidechainspoinitingoutwards
surfacepropertiesdependonsidechains
prolineis notfoundahelix determinepropensity ofahelixformationanditsinteractionswithotherpartsofproteinand
molecules
E iii i
B sheets
short ssaal nearlyfullyextendedsegments
H bonds areformed between a ssheetsoriented tochainsofbackbone
alignmentof2ormoreastrandsmakenearly 2 dimensionalsheets
sidechains aboveand belowasheetplane
priggata
baetermine
interactionswithin
proteinandmoleculesandpropensitytoform
organization
insamepolypeptidecanbeparallelorantiparallel
