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rFmo kipiiwdae: acenoS“ryd sueurrctt si alomyfrl eenfidd yb hte aptretn of rynhoged donsb ntbweee hte noima endhgryo adn bycxorla xgneoy atosm in eth eptpdie aobkbenc”. eia(mphss i)mne
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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Deu ot slneyigc' mlasl szie, ti saeecrt kk"sin" ni hte oainm diac uenceq.se heesT kniks era eended ot cotrleyrc fmro eht odesnrcya trsteruc.u
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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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wath si lecoanlg ? a oycdarnse otrenpi tsc.ururet
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$279$49I inkht ti sha sogimhetn to od wthi geynlci u(de ot tsi llsma zies ti nca tif in ymna plseac hwree herot naoim sadci can ont dan chnee ti svpriedo “arcututlrs ”oestscnpmac to eth clo,aegln ..ie utp a nikk ni eht aahlp xlh.e)i fI ngylice si desclpmia yb imnhgeost sel,e I nodt’ inkth nolerlcgapo- anc mrof ist rortcce cdyorneas teurtr.csu
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