<p>(A) Turbidity increases significantly as collagen self-assembles into fibrils. Experiments were conducted for a collagen concentration of 0.5 mg/ml (pH = 6.9 and 21°C). Open circles and error bars represent means and standard deviations from 3 replicate measurements. Inset schematics illustrate that the system begins as triple helical collagen molecules (more flexible than the rod-like schematic) and ends with well-ordered collagen fibrils (of which one small part is shown) that form a gel. (B) TEM image of a self-assembled collagen fibril formed under these conditions, showing the dark-light “D-banding” pattern expected for well-ordered fibrils.</p
Collagen fibril formation in vitro has been explained by resolving the process into nucleation and g...
Collagen molecules, self-assembled into macroscopic hierarchical tissue networks, are the main organ...
Collagen is the most abundant protein in human body and the major component of the extracellular mat...
AbstractType I collagen gels are routinely used in biophysical studies and bioengineering applicatio...
Collagen, the most abundant protein of connective tissues, in various forms has a wide applications ...
Collagen is a fibrous protein representing the main constituent of connective tissue in mammals, wit...
We present in situ studies on the self-assembly and dynamic evolution of collagen gels from semidilu...
We present in situ studies on the self-assembly and dynamic evolution of collagen gels from semidilu...
Most of the biological polymers that make up our cells and tissues are hierarchically structured. Fo...
School of Biological Sciences Type I collagen is a rod-like protein which self-assembles in a regula...
Three-dimensional fibrillar networks reconstituted from collagen I are widely used as biomimetic sca...
Collagen fibril formation has been studied in tissues by light and electron microscopy; in solution ...
Type I collagen is a major constituent of many biological tissues, including skin, bone, tendon and ...
Most of the biological polymers that make up our cells and tissues are hierarchically structured. Fo...
Self-assembly of rat tail collagen type I was investigated by means of turbidity measurements and mo...
Collagen fibril formation in vitro has been explained by resolving the process into nucleation and g...
Collagen molecules, self-assembled into macroscopic hierarchical tissue networks, are the main organ...
Collagen is the most abundant protein in human body and the major component of the extracellular mat...
AbstractType I collagen gels are routinely used in biophysical studies and bioengineering applicatio...
Collagen, the most abundant protein of connective tissues, in various forms has a wide applications ...
Collagen is a fibrous protein representing the main constituent of connective tissue in mammals, wit...
We present in situ studies on the self-assembly and dynamic evolution of collagen gels from semidilu...
We present in situ studies on the self-assembly and dynamic evolution of collagen gels from semidilu...
Most of the biological polymers that make up our cells and tissues are hierarchically structured. Fo...
School of Biological Sciences Type I collagen is a rod-like protein which self-assembles in a regula...
Three-dimensional fibrillar networks reconstituted from collagen I are widely used as biomimetic sca...
Collagen fibril formation has been studied in tissues by light and electron microscopy; in solution ...
Type I collagen is a major constituent of many biological tissues, including skin, bone, tendon and ...
Most of the biological polymers that make up our cells and tissues are hierarchically structured. Fo...
Self-assembly of rat tail collagen type I was investigated by means of turbidity measurements and mo...
Collagen fibril formation in vitro has been explained by resolving the process into nucleation and g...
Collagen molecules, self-assembled into macroscopic hierarchical tissue networks, are the main organ...
Collagen is the most abundant protein in human body and the major component of the extracellular mat...