| Range |
collagen molecular mass ≈3×10^5g/mole: measured critical concentration for self-assembly 0.42µg/ml
|
| 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.4 left column 3rd paragraphPubMed ID27559989
|
| Primary Source |
[19] Petruska J A and Hodge A J 1964 A subunit model for the tropocollagen macromolecule Proc. Natl Acad. Sci. USA 51 871–6 [20] Kadler K E, Hojima Y and Prockop D J 1987 Assembly of collagen fibrils de novo by cleavage of the type I pC-collagen with procollagen C-proteinase. Assay of critical concentration demonstrates that collagen self-assembly is a classical example of an entropy-driven process J. Biol. Chem. 260 15696–701PubMed ID14173005, 3316206
|
| Comments |
P.4 left column 3rd paragraph: "Using a molecular weight of collagen M≈3.0×10^5(g/mole) [primary source 19], and using the number density ρlower=0.17/µm^2, [investigators] obtain a conservative lower-limit estimate of the mass density of diffusing collagen of ρmass=0.08µg/ml. This is below the measured critical concentration for self-assembly of fully processed collagen into fibrils, 0.42µg/ml at 37°C [primary source 20], and more than four orders of magnitude below the critical concentration for pC [procollagen], which is at least 0.5 mg/ml [primary source 20]." Primary source [20] studied cultured human fibroblasts |
| Entered by |
Uri M |
| ID |
112910 |