Preview

Compare the Structure and Function of Collagen and Haemoglobin

Good Essays
Open Document
Open Document
701 Words
Grammar
Grammar
Plagiarism
Plagiarism
Writing
Writing
Score
Score
Compare the Structure and Function of Collagen and Haemoglobin
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.

Primary Structure; the number, type and sequence of amino acids The primary level of structure in a protein is the linear sequence of amino acids, formed by a condensation reaction. The primary structure of these proteins are very different. The haemoglobin molecule consists of four polypeptide (globin) chains, where as collagen is made up of three polypeptide chains wound round each other. In Haemoglobin there are a wide range of amino acid constituents in the primary structure, in contrast 35% of collagen’s primary structure is glycine. This difference in primary structure causes the proteins themselves to be different; due to the original different primary structure the haemoglobin protein is soluble in water whereas the collagen protein is not.

Secondary structure; Formed when the chain of amino acid coils or folds to form an alpha helix or beta pleated sheet. Haemoglobin is comprised of four polypeptide subunits, two with alpha helix secondary structure and two with beta pleated sheet form. All four components carry a heme group that

You May Also Find These Documents Helpful

  • 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
  • Powerful Essays

    Secondary: local regions of polypeptide chain fold into specific shapes (shapes arise from the bonding forces between amino acids close in proximity of linear sequence…

    • 2586 Words
    • 11 Pages
    Powerful Essays
  • Good Essays

    The quaternary structure is not necessary for all proteins. However, a quaternary protein is determined by how many polypeptide chains there are linked and the subsequent arrangement of the individual polypeptide chains, this determines the structure and function of the protein. (See figure…

    • 803 Words
    • 4 Pages
    Good Essays
  • Good Essays

    24. How does the hydrogen bonding in alpha-helices differ from the hydrogen bonding in the beta strands of polypeptides? a. alpha bonding is parallel to the axis of the polypeptide b. alpha bonding utilizes R-groups c. beta bonding utilizes R-groups d. beta bonding utilizes only the N-terminus for hydrogen bonding e. none of the above 25. A slight change in the pH environment surrounding a protein could affect the proteins’: a. b. c. d. e. amino acid sequence overall shape overall structure function b, c, & d…

    • 1088 Words
    • 5 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
  • Good Essays

    NST Exam 2 Study Guide

    • 3407 Words
    • 14 Pages

    General protein structure and chemical bonds: Contains hydrogen, oxygen, carbon, and nitrogen. Comprised of amino acids, a nitrogen (amino) group, a carboxyl (acid) group, a hydrogen, and a side chain (R) which determines protein function and name…

    • 3407 Words
    • 14 Pages
    Good Essays
  • Good Essays

    etched

    • 686 Words
    • 3 Pages

    A: Myoglobin has compressed globular tertiary structure that makes it suitable for transporting oxygen. Silk is very strong because it is composed of many parallel chains of beta-pleated sheets. Collagen is made up of a noticeably different secondary…

    • 686 Words
    • 3 Pages
    Good Essays
  • Good Essays

    AP I exam study guide

    • 372 Words
    • 2 Pages

    Know the four levels of structure of a protein and be able to describe them.…

    • 372 Words
    • 2 Pages
    Good Essays
  • Better Essays

    Western Blotting

    • 1563 Words
    • 7 Pages

    Western blotting is a technique in biological research that allows scientists to identify and quantify specific proteins among a protein mixture. The method that is used is a “protein mixture is applied to gel-electrophoresis in a carrier matrix (SDS-PAGE) to separate a protein by size and charge. Next, the separated protein-bands are transferred into a carrier membrane. The proteins are then accessible for anti-bonding in order to detect them” (Antibodies-online.com, 2012). Myosin is a muscle protein that is essential to animals for survival and has remained stable over time. The myosin light chain can be compared from different species for evolutionary divergence and similarities. The objective of this…

    • 1563 Words
    • 7 Pages
    Better Essays
  • Better Essays

    Emotional Spell

    • 1362 Words
    • 6 Pages

    Polypeptides are amino acids linked together by peptide bonds therefore creating a structure known as a polypeptide. A polypeptide backbone is a key contributor to the secondary structure of a protein due to the backbone to backbone hydrogen bonding interactions.…

    • 1362 Words
    • 6 Pages
    Better Essays
  • Good Essays

    Proteins are complex molecules that each has a very unique shape, structure and function. The shape of the proteins is held up by a chain of subunits called amino acids that are connected by peptide bonds. Protein structures are formed by four levels of folding. The primary structure is the linear sequence of amino acids. The secondary structure describes the folding of alpha helixes and beta pleated sheets. The tertiary structure represents the overall shape of the protein and the quaternary structure only occurs in a protein consisting of more than one amino acid chain. When the shape, the structure or the function of proteins is incorrect, it is likely because of some type of change in the sequence of the amino acids or whether a certain amino acid required is present.…

    • 581 Words
    • 2 Pages
    Good Essays
  • Better Essays

    Anatomy

    • 1604 Words
    • 7 Pages

    Collagen fibers that protect and reinforce the blood vessels and anchor it to surrounding structures…

    • 1604 Words
    • 7 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
  • Satisfactory Essays

    Antithrombin III

    • 194 Words
    • 1 Page

    Antithrombin III (AT III) is a glycoprotein and member of serpin super family protein .AT III inactivates more than a few enzymes of the blood coagulation system in Homo sapiens .The AT III gene on chromosome 1 encodes a glycoprotein of approximately 58 KDa MW .AT III is having 432 amino acids length with a single chain glycoprotein and 3 disulfide bridges and 4 carbohydrate side chains that report for 15% of the total mass .AT III also act as a mediator of heparin's anticoagulant activity with two to three days of biological half life [139]. Alfa AT III is also the most important form of AT III originated in blood plasma and has an oligosaccharide occupying each of its four glycosylation sites. A single glycosylation site remains always…

    • 194 Words
    • 1 Page
    Satisfactory Essays
  • Better Essays

    In effect human body use one molecule found in the red blood cell called haemoglobin, on the other hand the haemoglobin can be define as a molecule found in the red blood cell which deliver or transport oxygen to the rest of body muscles and tissues.…

    • 2199 Words
    • 9 Pages
    Better Essays

Related Topics