I ,eguirfd Xgey-lcYi-n si lcylcaihten erdiesndoc a iyrpr“ma onmai caid usetrutcr of a ”oreipnt icesn teh nneidftiio of a aimrPry serutctru of a rpetoin is a“ neialr cahni of nmoai adis.c” If uoy esms htiw eth rPriaym etusr,utrc sa in het qoineuts ,mtse oyu noactn rofm het dncrSaoey ttrrusuce of teh enip,otr hhwic si tmdreneedi yb the goydnbng-ohinred hhiwc urccos weebent het dpitepe oaebnckb, pdeeentndni of het R rgp.suo I ophe tsih deam sseen.
rmoF iediiapwk: nS“eaocyrd secrrttuu is floylrma defnedi yb the netrapt fo yondegrh sbdon entbwee het aionm dgheyrno dna albcryxo xnoeyg sotam in teh pidetpe bobnceka.” asi(mhpes men)i
From Molecular Biology of the Cell:
Biologists distinguish four levels of organization in the structure of a protein. The amino acid sequence is known as the primary structure of the protein. Stretches of polypeptide chain that form α helices and β sheets constitute the protein’s secondary structure. The full three-dimensional organization of a polypeptide chain is sometimes referred to as the protein’s tertiary structure, and if a particular protein molecule is formed as a complex of more than one polypeptide chain, the complete structure is designated as the quaternary structure.
ok ugsy nad i teoqu rmfo c.ccand1be:osfpas-/or/hol0e2tss.ie/geimpturtpteoo/eewmwihi/tr4swttsl
"%90 vhae na ibdtefinieal enicgte taomnuit
OLC 1A1 adn LCO A12
ssa
uce abralmon lnglaeoc snosi-cnlirgk aiv a eclgniy sobttsuintui in the aeonolpclgr lecmoule "
which msaen hatt IO has a ylcnieg iusstnttoiub and erohfetr its ablneu ot ofmr a sdrecoyna urct.uurtes
ueD ot 'nlsygice mslal s,zie ti rsatcee i"kksn" in hte nioma cida e.csueeqn Teseh skkni are ndeede to rleorccty rfmo the cenrsydao t.euucrstr
tOreh :sanwsre
-XGy-lY is ekoanbcb orf elcaglon ahlap ai.chn 3 colalneg ahpal sainhc ialprs to romf teiplr hleix. iylnGec ash on R r,upog nilwlaog ofr febyillitix nad oafitnmor of elrpit .ihelx No ncygeil nresvpte isth unntiosocu lsgrinp,ia erpinvtegn hte nfrtaoomi of lacelgno dncraoeys rtu.trecus
aellRc atht eahapslcilh-e dna ss-eteethab aer epmsexla fo dneyosrca reutts.cusr Tish anc eb oguthth fo a foaieinatstmn of the apahl ihx.el
otheArN yaw to etg at ti si vai tioinaenlm:i
A. renogydh obgdnni luwntdo laylre heangc niecs reineth lnnaiea nro cinegyl are Blpo .ar Gly t;g& lAa nudl'tsoh gachne owh opinerl is efmiiodd (I mena ti CLUDO, if etehr asw a rcites echinrnad or nmogeis,ht ubt tno a taegr ns)rw.eD a intnohg to itdnciae atht goalceln oendtgeradi si eertdal ni nreoepss to an AA ons.siitutbtu lo,As ni eht xentcto fo IO hc(wih is the nrnetegisp cm,aptilo)n ew dryalea kown tath hte orempbl tdos'en aveh gyntinha ot od wiht gaere,tonddi orme iwht het ngecah ni cn/.rterucstnft iuouE Hnsoetly dnto' .kwno
ere’Hs noe yaw ot ecf-ai-selormitesonp edcrds“eae ro-gdeobnhndy otir”:onfam mI’ not a bgi nfa fo htis elni fo ,oanisegnr btu actlehyncli nleaian as a esid gopru ash rmoe shdno*yger rof nlpoaiett ghyonedr nbindgo hant lniyceg:
lnaai:ne C—H3
gci:yenl —H
So, c”hlcl,nt“aeyi ailnnae dlouw prmeti ermo hnndedy-grboo tnfmao,iro hhicw ghimt llwoa uyo ot eiiamtlen thta oi.hcec
htaT s,aid it smsee ltoasm piissleobm ot urle out touit(hw yver clteicahn wlokdgnee or omes riveoddp ietaelnpxrme at)da tath eth shtllgiy leagrr nneiaal esod not piirma ongyhrde odnbngi wetbnee elcanglo celemslou iav tercsi )aap(itsl ceefe.einrnrt In lriespm mts,er enisc lneniaa is ,rgrlae ouy dolwu thnik htat it tusm ohomwse etfeirrne ihwt eht i-nnryohbegoddng that cusocr twih hte wtpie-ydl iyelgcn.
---
itltS*yrc gskepnia, ’tis ton eth munreb of dgyhrneos btu osal eht genthtsr fo hte pdoeli atht tcsieiltaaf heoyrgnd iondgnb: a droehygn odbun ot a ronsygtl eavrolncieegett euellocm eilk luoirenf iwll ”e“parap rmoe ioipstev ,nda stuh, gn-drboneydoh rmeo syonlgrt ihtw a erbany xongey acodprem( iwht a ronhdgey cnodetcen to a,cnbro for amle.)epx
uthreFr :igrande
From Molecular Biology of the Cell:
Hydroxylysines and hydroxyprolines are infrequently found in other animal proteins, although hydroxyproline is abundant in some proteins in the plant cell wall. In collagen, the hydroxyl groups of these amino acids are thought to form interchain hydrogen bonds that help stabilize the triple-stranded helix. Conditions that prevent proline hydroxylation, such as a deficiency of ascorbic acid (vitamin C), have serious consequences. (Emphasis mine)
From Molecular Biology of the Cell:
The primary feature of a typical collagen molecule is its long, stiff, triple-stranded helical structure, in which three collagen polypeptide chains, called α chains, are wound around one another in a ropelike superhelix (Figure 19-43). Collagens are extremely rich in proline and glycine, both of which are important in the formation of the triple-stranded helix. Proline, because of its ring structure, stabilizes the helical conformation in each α chain, while glycine is regularly spaced at every third residue throughout the central region of the α chain. Being the smallest amino acid (having only a hydrogen atom as a side chain), glycine allows the three helical α chains to pack tightly together to form the final collagen superhelix (see Figure 19-43).
I mgthi eb ieginkvtrnoh it bu,t H obnd ntrfmoioa fo aa's aeskm het oaedrnycs rsrtuuect of eth onrpeit a(lgcelno in htsi ).eacs ehT lGy ot aAl uuinststitbo esod etrlsu in elss H ndob o,rtmafino tub fo ldduviaini a'sa nto neebwet elolagcn oellcuesm t(ath gmtih eb eorm ofr aeryuqanrt uutrrsc)te
Pimarry curtterus = imaon dcai ynnceoqeeasduecSr ettcsurur = cserutrtu rmdefo twhi a inlges omian dcai qunesece e(bta padteel eth,es aaphl ieh,lx T ryette)irac tucterrsu = ellutmip nocedrsya stetrcruus aitnirtgnce etgetohr iue(ptllm taeb detplae etessh ktcasde on opt of heca reoth, ur)etyQer atrnac erturtucs = enptroi cerutsrut emdofr omrf gldinof fo lal iytarrte sruestctur ot mkae ingbnid ,teiss e.tc
iScne teh aenanli asw tpu in lepac of eht einGy,lc eht myrrpai rcustretu asw baulen ot frmo an hlpaa xilhe ncise paahl hlixe crrtsseuut need a pcualairrt qeenucse (gyl - -x y) ni droer ot ofrm dyrogehn nsobd to kpee eht hxeil .atlseb
what si ecognall ? a dnrsaecoy ertipon eu.ctrrtus
wehn oyu reoevm ,ecgylni eht msto unatnbda imnoa adic , mofr het rpcosuerr culoemel illw yuo gte a oepprr rocaeysdn rcrteutsu ? NO
yGl si lr,apo nleiAna si onaprnol nda dibco.rohphy sMeisesn oetnrinavnovsce mtouinat. ehseT sAA heva efrinfted ichalemc sotrrpeepi iwhhc laed ot strupidde neoptri flidgno (odayrnesc escuutrr.t) ailmSir ot lGu - aVl tbttoussniiu in kcileS Clel saseD.ie
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