| Range |
cross-sectional diameter ≈1.08: length ≈300 nm
|
| Organism |
Metazoa animals |
| Reference |
Rutenberg AD, Brown AI, Kreplak L. Uniform spatial distribution of collagen fibril radii within tendon implies local activation of pC-collagen at individual fibrils. Phys Biol. 2016 Aug 25 13(4):046008. doi: 10.1088/1478-3975/13/4/046008. p.2 right column 3rd paragraph & p.3 left column 3rd paragraphPubMed ID27559989
|
| Primary Source |
[11] Hulmes D J, Wess T J, Prockop D J and Fratzl P 1995 Radial packing, order, and disorder in collagen fibrils Biophys. J. 68 1661–70 DOI: 10.1016/S0006-3495(95)80391-7PubMed ID7612808
|
| Comments |
P.2 right column 3rd paragraph: "The number rate of precursor consumption necessary for growth, S, is determined by the area growth rate of fibrils: S=(dA/dt)/σ (4) where dA/dt is the net growth of fibril area for all fibrils in a bundle following fibril formation, and σ is the area per precursor. The cross-sectional diameter of one collagen molecule is approximately 1.08 nm [primary source], so that σ=0.916 nm^2." P.3 left column 3rd paragraph: "For collagen, with l≈300nm and d≈1.08nm, [investigators] have p[ratio of length to diameter]≈278." See Brown et al. 2014 PMID 25238208 p.8500 left column bottom paragraph: "At the molecular level collagen fibrils are linear aggregates of ∼300 nm long, ∼1 nm wide tropocollagen complexes with a distinctive triple-helical structure. [refs 8,9]" |
| Entered by |
Uri M |
| ID |
112905 |