Preview

Collagen vs. Haemoglobin

Good Essays
Open Document
Open Document
261 Words
Grammar
Grammar
Plagiarism
Plagiarism
Writing
Writing
Score
Score
Collagen vs. Haemoglobin
Haemoglobin’s quaternary structure is four polypeptide subunits (2 alpha and 2 beta chains) whereas Collagen’s structure is 3 polypeptide chains wound around each other like rope.
Haemoglobin has a prosthetic group – each chain contains a haem group (Fe2+) but collagen has no prosthetic group.
Haemoglobin is made of a wide range of amino acid constituents in its primary structure whereas approx 35% of collagen’s primary structure is just one type of amino acid – glycine.
Much of a Haemoglobin molecule is wound into alpha helix structures but collagen’s molecule mainly consists of left-handed helix structures.
Haemoglobin’s function is as a transport molecule and carries oxygen around the body. In contrast collagen’s function is as a structural molecule and to give strength to many cells including artery walls, tendons, bones, and cartilage. This is why it is important that Haemoglobin is soluble (so it can travel around the body in the blood) and Collagen is insoluble (wouldn’t be able to provide support otherwise as would always dissolve). Haemoglobin’s shape is important so that red blood cells become biconcave disks which can easily travel around the body and bind with oxygen.
Haemoglobin is a globular protein meaning its 3D feature is to roll up into balls, yet collagen is a fibrous protein so its 3D feature is to form fibres.
Haemoglobin molecules to not bond with each other. However, collagen molecules form covalent bonds between molecules called cross-links which are staggered along the collagen molecules, both increasing strength and forming a fibril. Many fibrils joined together make a collagen

You May Also Find These Documents Helpful

  • Good Essays

    Case Study: Dr. Pauling

    • 777 Words
    • 4 Pages

    Proteins have lively and complex structures. The purpose of a protein is decided by its structure; a change in the proteins activity level causes a change in some part of the proteins shape. In the experiment it is clear that the hemoglobin molecules of people with sickle cell anemia traveled at a different rate and therefore ended up at different places on the electrophoresis gel. Hemoglobin is a protein in red blood cells that carries oxygen through the body. Sickle cell hemoglobin is not like normal hemoglobin. It…

    • 777 Words
    • 4 Pages
    Good Essays
  • Satisfactory Essays

    9. Tissue Plasminogen Activator (TPA), Heparin, and Warfarin are all fibrinolytic substances. Think about what the suffix "-lytic" means and…

    • 464 Words
    • 2 Pages
    Satisfactory Essays
  • Good Essays

    Biology 130l Exam Review

    • 2549 Words
    • 11 Pages

    Molecular weight, overall shape and degree of branching in the final polysaccharide structure. Amylose is unbranched and helical, where glucose units are joined by a(1-->4) linkages. Amylopectin has straight, branched sections from a(1-->6) linkages. Glycogen is similar to amylopectin, but more highly branched.…

    • 2549 Words
    • 11 Pages
    Good Essays
  • Good Essays

    If the polypeptide chain form beta pleated sheets (folded chains running parallel to each other) then the hydrogen bonds between the CO (carboxyl group) and NH (amino group) occurs between two separate beta pleated polypeptide chains (see figure 10)…

    • 803 Words
    • 4 Pages
    Good Essays
  • Good Essays

    From my diagram I can observe the quaternary structure is 3 helical polypeptides which are looped around and is held by hydrogen bonds. The 3 stranded molecules runs parallel to others and the disulphide cross-linkages between the r-groups of the amino acid holds the molecules together forming fibres. Collagen molecules forms covalent bonds which are called cross links, with other collagen molecules next to it. The cross-links that form are shocked along the collagen molecules and adding to the strength of the molecules. This structure called a collagen fibril. Many fibrils together form a collagen fibre.…

    • 934 Words
    • 4 Pages
    Good Essays
  • Good Essays

    Chapter 17 Study Guide

    • 920 Words
    • 4 Pages

    Hemoglobin is an oxygen-binding pigment that is responsible for the transport of most of the oxygen in the blood.…

    • 920 Words
    • 4 Pages
    Good Essays
  • Satisfactory Essays

    Why is it significant that keratin and collagen are fibrous proteins and myoblobin and hemoglobin are globular proteins?…

    • 2555 Words
    • 14 Pages
    Satisfactory Essays
  • Good Essays

    An example of a polymer, is a protein. The monomer used to make up is an amino acid. When two amino acids join together a dipeptide is formed, this is then made into a polypeptide chain by the joining of additional amino acids, it finally becomes a protein when more than one of these polypeptide chains link to one another in a condensation reaction. Proteins have a variety of functions, these functions are determined by their shapes. For example, haemoglobin, this is a substance in the blood that transports oxygen from the respiratory organs to the rest of the body and returns the waste product carbon dioxide to be exhaled. In order to do so it must therefore have a specific shape reflecting its function; it must be folded in a particular way that allows oxygen and carbon dioxide to bind to it, and as much as possible. One haemoglobin molecule can carry four oxygen molecules each bound to a specific site. Haemoglobin has a quaternary structure. Most of the amino acids in haemoglobin form alpha helix eps, connected by short non-helical segments. Hydrogen bonds stabilise the helical sections inside this protein, causing attractions within the molecule, folding each polypeptide chain into a specific shape.…

    • 808 Words
    • 4 Pages
    Good Essays
  • Good Essays

    Haemoglobin is a transport protein that carries oxygen from the lungs to the tissues and carries carbon dioxide from the tissues back to the lungs. In order to function most efficiently, haemoglobin needs to bind to oxygen tightly when the oxygen concentration is high in the lungs and be able to release oxygen rapidly in the relatively low partial pressure in the tissues. I will be comparing the structure and function of haemoglobin with the structure and function of collagen, which is a structural protein. Collagen’s functions are quite different from those of globular proteins such as enzymes; tough bundles of collagen called collagen fibers are a major component of the extracellular matrix that supports most tissues and gives cells structure from the outside. Collagen is also present in certain cells as it has great tensile strength, and is the main component of fascia, cartilage, ligaments, tendons, bone and teeth.…

    • 701 Words
    • 2 Pages
    Good Essays
  • Better Essays

    The structure involves the folding and coiling of the polypeptide chain to give protein its 3-dimensional shape. Protein has two types of secondary structure; the alpha (α) helix and the beta (β) pleated sheet, refer to figure 3. The α helix is coiled and held together by a hydrogen bond in the polypeptide chain, whereas the beta sheet has pleated sheets of the "polypeptide chain lying side by side and connected by hydrogen bonds"(Campell,Biology,pp82 )…

    • 1093 Words
    • 5 Pages
    Better Essays
  • Good Essays

    Tissues In The Human Body

    • 1479 Words
    • 6 Pages

    This type of tissue is the rubbery protein constituent of bone, cartilage, tendon, and other connective tissue. It is transformed into gelatin by boiling. Collagen is a protein composed of amino-acids, which are in built of carbon, oxygen and hydrogen.…

    • 1479 Words
    • 6 Pages
    Good Essays
  • Good Essays

    mastering biology

    • 449 Words
    • 2 Pages

    The principal fiber type is collagen -- the most abundant protein in the body -- which confers tensile strength with flexibility.…

    • 449 Words
    • 2 Pages
    Good Essays
  • Better Essays

    Rnai

    • 3925 Words
    • 16 Pages

    McMahon, L., Muriel, J.M., Roberts, B., Quinn, M., and Johnstone, I.L. (2003). Two sets of interacting collagens form functionally distinct substructures within a Caenorhabditis elegans extracellular matrix. Mol Biol Cell 14, 1366-1378.…

    • 3925 Words
    • 16 Pages
    Better Essays
  • Good Essays

    2) Identify the reason for [A] myoglobin and [B] fetal haemoglobin having oxygen binding curves different from…

    • 680 Words
    • 3 Pages
    Good Essays
  • Powerful Essays

    Hemoglobin Model

    • 365 Words
    • 2 Pages

    Hudson-Miller, S (n.d.) “ An explanation of the cause of differences of oxygenated and deoxygenated hemoglobin.…

    • 365 Words
    • 2 Pages
    Powerful Essays

Related Topics