Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm.
Fibers composed of type I collagen triple helices form the organic scaffold of bone and many other tissues, yet the energetically preferred conformation of type I collagen at body temperature is a random coil. In fibers, the triple helix is stabilized by neighbors, but how does it fold? The observat...
I tiakina i:
| Ngā kaituhi matua: | , |
|---|---|
| Hōputu: | Artigo |
| Reo: | Inglês |
| I whakaputaina: |
Public Library of Science (PLoS)
2007-01-01
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| Rangatū: | PLoS ONE |
| Urunga tuihono: | http://europepmc.org/articles/PMC2000351?pdf=render |
| Ngā Tūtohu: |
Kāore He Tūtohu, Me noho koe te mea tuatahi ki te tūtohu i tēnei pūkete!
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