where is collagen made in the human body
Collagen
The molecular and packing structures of collagen have eluded scientists over decades of research . The first evidence that it possesses a regular structure at the molecular level was presented in the mid-1930s . Since that time , many prominent scholars , including Nobel laureates Crick , Pauling , Rich and Yonath , and others , including Brodsky , Berman , and Ramachandran , concentrated on the conformation of the collagen monomer . Several competing models , although correctly dealing with the conformation of each individual peptide chain , gave way to the triple - helical `` Madras '' model of Ramachandran , which provided an essentially correct model of the molecule 's quaternary structure although this model still required some refinement . The packing structure of collagen has not been defined to the same degree outside of the fibrillar collagen types , although it has been long known to be hexagonal or quasi-hexagonal . As with its monomeric structure , several conflicting models alleged that either the packing arrangement of collagen molecules is ' sheet - like ' or microfibrillar . The microfibrillar structure of collagen fibrils in tendon , cornea and cartilage has been directly imaged by electron microscopy . The microfibrillar structure of tail tendon , as described by Fraser , Miller , and Wess ( amongst others ) , was modeled as being closest to the observed structure , although it oversimplified the topological progression of neighboring collagen molecules , and hence did not predict the correct conformation of the discontinuous D - periodic pentameric arrangement termed simply : the microfibril . Various cross linking agents like L - Dopaquinone , embeline , potassium embelate and 5 - O - methyl embelin could be developed as potential cross-linking / stabilization agents of collagen preparation and its application as wound dressing sheet in clinical applications is enhanced .
The molecular and packing structures of collagen have eluded scientists over decades of research . The first evidence that it possesses a regular structure at the molecular level was presented in the mid-1930s . Since that time , many prominent scholars , including Nobel laureates Crick , Pauling , Rich and Yonath , and others , including Brodsky , Berman , and Ramachandran , concentrated on the conformation of the collagen monomer . Several competing models , although correctly dealing with the conformation of each individual peptide chain , gave way to the triple - helical `` Madras '' model of Ramachandran , which provided an essentially correct model of the molecule 's quaternary structure although this model still required some refinement . The packing structure of collagen has not been defined to the same degree outside of the fibrillar collagen types , although it has been long known to be hexagonal or quasi-hexagonal . As with its monomeric structure , several conflicting models alleged that either the packing arrangement of collagen molecules is ' sheet - like ' or microfibrillar . The microfibrillar structure of collagen fibrils in tendon , cornea and cartilage has been directly imaged by electron microscopy . The microfibrillar structure of tail tendon , as described by Fraser , Miller , and Wess ( amongst others ) , was modeled as being closest to the observed structure , although it oversimplified the topological progression of neighboring collagen molecules , and hence did not predict the correct conformation of the discontinuous D - periodic pentameric arrangement termed simply : the microfibril . Various cross linking agents like L - Dopaquinone , embeline , potassium embelate and 5 - O - methyl embelin could be developed as potential cross-linking / stabilization agents of collagen preparation and its application as wound dressing sheet in clinical applications is enhanced .