I ugfeidr, -ylc-gYeniX
is lehyanctlic eosidrendc a pyrirma“ ianom cdia rtesucutr fo a iptern”o enics teh iitdeonnfi of a yirrmaP curtrutes fo a perntoi si a“ rlaein hcani of onima ais”dc. fI uoy esms ihwt teh raymPri ,tceuustrr sa in het esitqnou met,s yuo nnotca mfro teh Scerdaony cuetusrtr fo het noer,itp whhci si edidenermt yb teh doidnynebogg-nrh hcwih csruoc teneewb het peeipdt nebcabok, ennedetnidp of eth R ugpro.s I pheo ihts dmea nes.es
omrF ipkideiwa: roacyeSd“n reuscttur is lymlorfa dineefd by eht erntapt fo yndeghro bnsod eebentw eth onmia drnoyheg and lcorybxa yeonxg soatm ni teh piepted kocnabeb”. ms(iphase n)iem
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 ygus nad i queot mfro ph/2ot0ritmrop:cwfsdcnwta4eoegsce/pbemieul1ttrsoi/te-eithow/a.l.ss/s
"9%0 aehv an adenitefibil cenetig mitnaout
COL 1A1 dan CLO 2A1
uaessc
bonaarml caonellg lonscs-kngrii vai a cengyil tiinbttuuoss ni the gloolencpar cloumeel "
hciwh samen thta OI has a yignecl itosnstuuibt dna feoerhrt tis eulbna to ormf a rasycndeo ttcuruu.rse
euD to gslie'ycn smlla ,iesz it atrecse ""snkik ni teh imoan diac nceseequ. eTseh nkski rea eedend ot yceorrlct frmo het cdyoarsne .uutstrcre
rhteO wernas:s
-y-XYlG is ecbkbnao rof alcgleon hlapa nhic.a 3 elonalcg lphaa nsiahc iprasl to from itprle eihx.l lcGyien sah no R p,guro nioglalw rfo tyixlelfibi nda mfonartio fo elript iehl.x oN legnicy nseevrtp sthi ouutcsnoni alpsiing,r gpivntneer het itamoofrn fo gcaeloln acdsneoyr .tesrrucut
Rellca atth seahhiecpll-a dan ste-tebashe era semxpael of nsoydaerc r.steutuscr sThi cna be hgutoht fo a aeonfiitstnma fo hte alhap elh.ix
trAeoNh awy ot tge ta ti si avi itnin:aoielm
.A dygonher ndonibg noudltw aelrly ecngah encis hitrene naeinla nor iylgnce era r Bla.op Gyl g&t; laA tndh'luso egnhca woh pielnro is ioiedmdf (I mane ti OCL,DU fi theer asw a rtesci aehdircnn or ,onhesmgti btu nto a trage e .)wasrDn tnhgino ot icnatied ahtt llagnceo dagereinotd is tdelera in pesrnseo to na AA sisnuotttbui. s,lAo ni eth ecntxto fo IO wih(ch is the tingsneerp polm,c)aitn we eraydla onwk hatt eth eprlmbo dsnte'o aveh niahyngt to od htwi ndeerao,dgti omer ithw hte ehcang ni fti.nsucur ctnE/oertu yeloHsnt nt'od nokw.
’eHres neo yaw to mere-ftopse-snaiicol sdeecare“d og-enrdnodbyh ra:oot”nfmi mI’ nto a big fna fo htis inel of aog,rennsi tub hiycclateln nelaain
sa a eisd guorp ahs moer yrdgeh*nos rof einpattlo nohgreyd gnionbd athn egynlci
:
nli:anea
HC—3
ngl:yice
—H
o,S h“llceya”ti,cn inaaenl
lduow peitmr erom odyneongrdbh- if,noratom wchhi hmtig wolal uoy ot iltenamie atht iecc.ho
That a,isd it essme osmalt seomipbisl to rleu uto uhitow(t yrev liencatch newldogek ro semo revopddi etxnmaepirel dt)aa tath teh igyllsth agrler ennlaai
odse ton iraimp egndoyhr dibgnon weteenb cenallog slolceume via cersit li(taspa) en.etnicrfree In elipsrm sr,met csnei aeilnna
is glre,ra uyo ldwou tkihn taht it stum moseowh rienrtfee whti eth eonoidgnrndghb-y ttah srccou twhi eht diptwye-l genycli
.
---
rct*tiSyl ,iankesgp it’s nto eth benurm of gneryohsd btu asol hte hstnretg of hte dpoeli ahtt ifslteticaa hornyegd bdgi:onn a dyeorhgn odbnu ot a sroyngtl gaecereloevntti oemeulcl leki louenfri liwl ear“pap” eorm itoespvi adn, uh,st rnhygnd-doboe mero ngoyltsr htiw a arbyne nogyxe op(rcmeda wtih a hdeoryng nodetncce ot roca,nb fro e)xmea.lp
turrehF i:rdaeng
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 ghmti eb ronhntgiviek ti utb, H donb ritofamno fo 'asa emsak teh ernsdocay tcrurseut of the tornpei caleo(nlg ni ihst .eac)s ehT lGy ot aAl tuiouttnbssi deos srtelu ni slse H nbdo ,iafoomrnt utb fo liudinadiv a'sa ont eewbten golclnae eslmeuolc a(tht gthim eb roem rfo ynreaqraut )tcurrtues
mrirPya teruuctrs = mnioa diac ce qeancyuereSdosn etrcuruts = tucsrreut rodmef hwit a lisneg ioamn icda snqeueec teb(a paeeldt ,eseht alahp hilx,e r)riTtey atce trcuutres = lelutpim osrcaeydn custuesrtr ttriagencin oethetrg ulmt(lipe atbe deapetl sshete etskadc on tpo fo heac e,troh y ueentrrtQcr)aa trstceuru = piroten surcettur omrefd rfom olfdgin of all yettrari esuturctrs ot keam ininbdg ,iests .tce
ncSie eth nnilaae wsa put ni aeclp of teh yniGc,le het mpyrria cettuursr was neblau to mfro an lpaha hxeil secni aalph heilx sretsucurt eend a aiurptcral nqeesceu lgy( - x- y) ni erdor ot ormf ehdnogyr obnsd to epke het hilex tslbea.
hawt si gleocnla ? a ersdnaoyc eoinprt .ucesrtutr
nhwe ouy emoevr ,cigelny het tsom ntuaabnd naoim iadc , mfro eth crrrusoep cmoellue lilw ouy gte a reoppr osyedrcna tcrueutrs ? ON
ylG is l,arop eanAiln si rnoonpal nad oich.rbpdhoy esiMesns eanonvncotseirv nitmauto. Tseeh sAA veah effnditer leiachmc tpeeorspri chiwh lead to pdtdeiurs neiotrp dfiolgn cna(eysrdo .uutc)tsrre arliimS ot Gul - laV obuntutiitss ni kcileS Cell si.seDea
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