I ,rfiedgu X--ncYegily si litceylcanh rideoncesd a priamy“r ainmo dcai turrceust of a inpe”otr inesc eth indtefioni fo a arimyrP cruuerstt of a noirtep is “a earnli hacni fo amoni as.ic”d fI yuo msse thiw teh arryimP trce,ruuts sa ni teh qnusieot stm,e you cnanto form eht draeSncoy tetruscur fo the eto,pnir chwhi si menrteeidd by teh ghedgonnybdo-rin ihhcw uocscr beweten the deieppt ebboncak, endeedintnp of eht R opgur.s I ohep isth dema en.ses
Frmo iikdpeawi: oanSdy“rec utrrcuste is raolmlyf nedidef yb eth eatrpnt fo yodhrneg obnsd tweebne hte oamin yrondhge and yaoblcxr xnygoe smoat in the petepdi bbekaocn.” sipmsh(ae nme)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.
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C 1A1 dan COL A21
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iwchh sneam ahtt OI sha a yngicle siubtttoisnu dna orfhrtee its ablnue to orfm a yrasdeonc rttsueucur.
euD ot csyieln'g smlal s,zei it teraesc nkk"i"s in hte nmoia cida ees.qncue seThe iknsk aer edndee to lcrycerot ormf the eodrnaysc rceutts.ru
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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).
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Sneci hte ianelan asw tup in eclpa fo eth Gceiln,y hte rpmariy uterrcstu swa lbnaeu to omrf an lhapa ehlix csine palha xhlei sttsrcuure nede a acirtaulpr qenueesc l(gy - -x )y ni rrdoe ot form ngordyhe obdns to peek eht lixhe bsl.aet
hawt si lnlaogce ? a yacsdoner ipoetnr ut.rtcuser
whne ouy oemrev n,giceyl hte smot baatnund amoin diac , fmor eht ourrsecpr uocemlel ilwl yuo get a ropepr earcdnyos urturstec ? ON
lyG is olarp, ielannA is rpolnnoa adn .yobdhpocirh sMesesin vsrnconntaievoe .aounttim hTsee AsA veha irtfenfed laimchec persepoitr cwhih lead to tdsdureip ipeonrt gldonif y(ecsdoanr cu.es)rttur irmiSal ot Gul - laV stiutosutibn ni liekcS eCll esei.Dsa
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