Related Experiment Video
Updated: Jul 30, 2026
07:54
In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
Published on: September 20, 2012
Stereochemistry of collagen
1Mathematical Philosophy Group, Indian Institute of Science, Bangalore.
International Journal of Peptide and Protein Research
|January 1, 1988
Summary
The collagen triple-helix structure was elucidated through decades of research, revealing key roles for glycine and hydroxyproline. This work confirmed vitamin C
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Biology
Background:
- The collagen triple-helix is a fundamental protein structure in connective tissues.
- Early research in the 1950s proposed initial models for collagen's molecular structure.
- Understanding collagen's conformation is crucial for comprehending its biological functions.
Purpose of the Study:
- To review the historical development and refinement of the collagen triple-helix model.
- To account for experimental and physicochemical data related to collagen structure.
- To explore the role of specific amino acids and stabilizing interactions.
Main Methods:
- Analysis of X-ray diffraction patterns.
- Energy minimization techniques.
- Physicochemical data interpretation (optical, hydrodynamic).
- Review of experimental findings from 1952-1978.
Main Results:
- Established the coiled-coil triple-helix structure with approximately 3.3 residues per turn.
- Identified glycine as every third residue and accommodated proline/hydroxyproline.
- Resolved the hydrogen bonding controversy, including the role of water molecules.
- Demonstrated hydroxyproline's crucial role in stabilizing the triple helix via water-mediated bonds.
Conclusions:
- The refined collagen triple-helix model satisfactorily explains primary structure, X-ray data, and physicochemical properties.
- Hydroxyproline's contribution to collagen stability is confirmed through detailed structural insights.
- The findings support Pauling's theory on vitamin C enhancing immunity.
Related Concept Videos
02:52Stereoisomerism
Isomerism in Complexes
Isomers are different chemical species that have the same chemical formula.
Transition metal complexes often exist as geometric isomers, in which the same atoms are connected through the same types of bonds but with differences in their orientation in space. Coordination complexes with two different ligands in the cis and trans positions from a ligand of interest form isomers. For example, the octahedral [Co(NH3)4Cl2]+ ion has two isomers (Figure 1) In the cis...
Isomers are different chemical species that have the same chemical formula.
Transition metal complexes often exist as geometric isomers, in which the same atoms are connected through the same types of bonds but with differences in their orientation in space. Coordination complexes with two different ligands in the cis and trans positions from a ligand of interest form isomers. For example, the octahedral [Co(NH3)4Cl2]+ ion has two isomers (Figure 1) In the cis...
01:56Structural Protein Function
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...
02:33Stereoisomerism of Cyclic Compounds
In this lesson, we delve into the role of ring conformation and its stability, which determines the spatial arrangement and, consequently, the molecular symmetry and stereoisomerism of cyclic compounds. 1,2-Dimethylcyclohexane is used as a case study to evaluate the possible number of stereoisomers. Here, given the multiple (n = 2) chiral centers, there are 2n = 4 possible configurations that lack a plane of symmetry, as the ring skeleton exists in a non-planar chair conformation. In addition,...
01:13Collagens are the Major Structural Proteins of ECM
Three main types of fibers are secreted by fibroblasts: collagen fibers, elastic fibers, and reticular fibers. Collagen fiber is made from fibrous protein subunits linked together to form a long, straight fiber. Collagen fibers, while flexible, have great tensile strength, resist stretching, and give ligaments and tendons their characteristic resilience and strength. These fibers hold connective tissues together, even during the body's movement.
Connective tissue proper includes loose...
Connective tissue proper includes loose...
01:11Fibril-associated Collagen
Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
01:05Type IV Collagen of Basal Lamina
Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
A type IV collagen molecule has six alpha chains which can exist in...
A type IV collagen molecule has six alpha chains which can exist in...