structure of collagen slideshare

Connective TISSUE is composed of ground substance, structural fibers and proteoglycans. What is collagen? collagen fibres. 1) [7,16]. It forms the bulk of dentin, whereas peritubular dentin is more variable, according to species, and location examined. Peptidoglycan Definition. It is the basic protein globin that varies in amino acid composition and sequence in different species. 12. Answer (1 of 2): Despite the typical oversimplified explanations of what collagen is, it’s actually quite a bizarre molecule. Collagen fibers are the most abundant fiber type. This article emphasizes in the complex ECM structure as to provide a better understanding of its dynamic structural and … Blood is pumped from the heart in the arteries. 1. 1000 amino acid residues . A major component of the extracellular matrix is the protein collagen. It is one of the most plentiful proteins present in mammals and it is responsible for performing a variety of important biological functions. Biological importance of proteins Collagen is a structural support for most tissues in the body as the extracellular matrix, and is particularly abundant in connective tissue. The defining feature of collagen is an elegant structural motif in which three parallel polypeptide strands in a left-handed, polyproline II-type (PPII) helical conformation coil about each other with a one-residue stagger to form a right-handed triple helix (Figure 1). Collagen Molecular Structure. Proteins are the macromolecules responsible for the biological processes in the cell. Collagen fibrils display a 100-120 nm diameter . The fibrous capsule, for most joints, is a firm structure consisting of dense connective tissue that invests the entire joint and usually inserts into the bones close to the articulating surfaces. At this point, it essentially becomes gelatin. Grows hair: The roots of hair follicles attach to the dermis. Collagen fibers are made up of many subunits, called collagen fibrils, that appear striated under electron microscopy. Dense regular connective tissue - the tissue shown has a dense, regular arrangement of collagen fibers; the cells present are fibroblasts NOT squamous epithelial cells. The linkage of GAGs such as (heparan sulfates and chondroitin sulfates) to the protein core involves a specific trisaccharide linker: Some forms of keratan sulfates are linked to the protein core through an N-asparaginyl bond.. Both contain a high amount of the smaller amino acid residues, glycine and alanine, which makes the a-helical structure possible. Surprisingly, even though the NPC spans two membranes (the outer- and inner-nuclear membrane), only four of the human Nups contain transmembrane (TM) domains, namely Ndc1, Gp210, TMEM33 and Pom121. Ø The basic unit of a single immunoglobulin consists of four linear polypeptide chains. The amino acids proline and hydroxyproline occur in large amounts in collagen, the protein of the connective tissue of animals. The collagen molecules themselves are made from 3 individual polypeptides or strings of amino acids. G N Ramachandran is an Indian biophysicist who was known for his work that led to his creation of the Ramachandran plot for understanding peptide structure. protein structure and function.pptx. (antibodies), attack (toxins), hormones (insulin, growth hormone) and structure (collagen). In the structure of tendons and ligaments, for example, collagen appears as parallel N H COOH H proline a-amino group a carbon a PROBLEM 24-1 Draw three-dimensional representations of the following amino acids. The primary structure of collagen is the Triple Helix. This type of collagen is a long rope-like structure. This is created with three polypeptide chains that are almost braided together. Every third amino acid is a glycine, which fits perfectly into the helix. collagen family have one characteristic feature: a right-handed triple helix composed of three a-chains (Fig. - It gives proteins globularity rather than linearity. Secondary Structure. Intertubular dentin is a type I collagen-rich structure. It is a protein composed primarily of the amino acids glycine & proline, and it also contains sugar groups. All pro-teins contain C, H, N, O some S, P, Fe, Zn, Cu. Collagenis a member of a family of naturally occurring proteins. 8. The salient features of this structure are: i. In the proposed review paper, the structure, preparation, and properties of several collagen based materials have been discussed in general, and detailed examples of collagen cross-linking methods have been drawn from scientific literature and practical work. are found with collagen, which is the other major structural protein in animals (bones, teeth, and con-nective tissue). This type of structure is found in many proteins in combination with other structures. Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution. Fibrous cartilage. Acidic hydrolysis yields 20 different α-amino acids (L-form), which are encoded by the genetic code and which constitute the … These might be formed by three identical chains (homotrimers) as in collagens II, III, VII, VIII, X, and others or by two or more different chains (heterotrimers) as in collagen types I, IV, V, VI, IX, and XI. Chemistry of Proteins Definition: Proteins are organic compounds with a high molecular weight formed of carbon, oxygen, hydrogen and nitrogen and may also contain sulfur, phosphorus coloring non-protein organic groups and metal ions. The sequence is a repeating pattern of glycine-proline-X, where X can be any amino acid. BASIC STRUCTURE OF COLLAGEN • Composed of 3 polypeptide alpha chains coiled around each other to form the tripe helix configuration- homotrimeric or heterotrimeric •Depending on the type of collagen the molecule may be made up of either 3 identical α chains or 2 or 3 different α chains. It is referred to as the manufacturing and the shipping center of the cell. Tropocollagen Fibrous protein consisting of three strands twisted together and containing large amounts of glycine, proline, and hydroxyproline. (a) L-phenylalanine (b) L-histidine (c) D-serine (d) L-tryptophan Gelatin is made from collagen, which is a structural protein com- It is the most abundant protein in mammals - 25% of total protein mass! (Ramachandran & Ramakrishnan 1976) 11. Hyaline cartilage. The helix forms because of the regular amino acid sequence of the strands. These 3 types of cartilage contain mostly the same compounds, such as type II collagen—a protein that helps “hold the body together” by providing structural support. Type IV collagen, which forms a meshwork structure, is restricted to the basement membrane of the tendon blood vessels . This article reviews its structure and functions. Collagen occurs in many places throughout the body. structure in proteins) •dextrorotatory helix •gradual rising •3,6 AA/turn •stabilization by intrachain hydrogen bonds Comparison of collagen helix to the α-helix, which represents the most common secondary structure in proteins. Dense Connective Tissue. I. Previous Page Next Page. However, these trimers do not assemble into parallel, crosslinked arrays to form ﬁbrils. Collagen Fibrous protein composed of three strands of tropo-collagen. Routine stain for liver and kidney biopsies. Over 90% of the collagen in the body, however, is type I So far, 28 types of collagen have been identified and described. Amino acids are the building block of all proteins. Elastic cartilage. Globin is rich in Histidine and lysine. Structure of Immunoglobulins. Gopalasamudram Narayana Ramachandran(8 October 1922 – 7 April 2001) is an Indian biophysicist and crystallographer who, along with Gopinath Kartha, worked out the triple helical structure of collagen. This cyclic structure lends additional strength and rigidity to proline-containing peptides. They consist at their most basic level of a chain of amino acids, determ… Collagen provides structure to the skin, and works hand in hand with another protein, called elastin, to allow skin the flexibility it needs to stretch and return to its original state as your body moves. One of the most noticeable functions of collagen is the support it provides for your skin. They have a high tensile strength but are also flexible. In collagen, the collagen helix, or type-2 helix, is a major shape in secondary structure. It consists of a triple helix made of the repetitious amino acid sequence glycine-X - Y, where X and Y are frequently proline or hydroxyproline.A collagen triple helix has 3.3 residues per turn. Proteins are macromolecules made up of monomers called amino acids. Within the capsule are thick bands or condensations of parallel collagen fibers known as ligaments. Differences have been also … Ø These peptide chains are named as two identical Heavy Chains and two identical Light Chains. The Golgi apparatus or the Golgi body or Golgi complex or simply Golgi is a cellular organelle present in most of the cells of the eukaryotic organisms. Consequently, the ECM functions to respond to the tensile, shear, and compressive forces that are experienced by cartilage during mechanical use such as normal gait or weight-bearing movements. (antibodies), attack (toxins), hormones (insulin, growth hormone) and structure (collagen). Biosynthesis of collagen cross-links: ... gives the collagen fibre its high tensile strength. Structure and Function of Proteoglycans. They are polymers formed of subunits called amino acids linked together by peptide linkage.. All pro-teins contain C, H, N, O some S, P, Fe, Zn, Cu. But variations in the structure of each type … Histology of Connective Tissues - 4. Elastin is roughly 1000 times more flexible than collagens; thus, the main function of elastin is the elasticity of tissues. The BM structure is thought to be set by laminin and collagen IV. • Poor perfusion due to diabetes or atherosclerosis. The five most common types are: • Collagen I: skin, tendon, vascular ligature, organs, bone (main component of the organic part of bone) Beneath the epidermis is the basement membrane (also known as the dermo-epidermal junction); this narrow, multilayered structure anchors the epidermis to the dermis. Type Structure Tissue Distribution I Fibril Bone, ligament, skin, tendon, artery walls, cornea II Fibril Cartilage III Fibril Reticular ﬁbers IV Sheetlike network Basement membrane Collagen is the most abundant class of proteins and pound for pound some are as strong as steel. This structure is shown in the graphic on the left. Dense connective tissue is for strength! On hydrolysis these proteins yield only constituent amino acids. Science. Importance. Ground substance supports cells, binds them together may be solid, fluid or gel. Ø The heavy chains are long and heavy with a molecular weight of 50 – 70 kDa. The collagen (mainly type II), acts to constrain the proteoglycans and helps it hold its structure. The basic properties of collagen are rigidity and resistance to stretching. Bones and teeth are made by adding mineral crystals to collagen. This is the part of molecular biology course that would describes you about Structure and Function of Nucleic Acid Individual precursor chains are synthesized on membrane-bound polyribosomes. Proteoglycans are ubiquitous molecules that function as critical components of the extracellular matrix. Classification of Proteins. Structure of the skin. The term amino acid is short for alpha-amino carboxylic acid. Depending on the class of collagenase, once the tissue is exposed to collagenase enzymes, it will bind to and cut either the ends of a collagen fibril or the middle of a collagen monomer. Once the structure of the triple helical is cut, they begin to unravel and denaturation takes place. Golgi Apparatus Definition. They are classified into three types; fibrous, globular and derived protein. Ground substance supports cells, binds them together may be solid, fluid or gel. Stretches or strands of proteins or peptides have distinct, characteristic local structural conformations, or secondary structure, dependent on hydrogen bonding. (a) The repeating tripeptide sequence Gly-X-Pro or Gly-X-Hyp adopts a left-handed helical structure with three residues per turn. Amino acids are the building blocks of proteins; therefore, it is no surprise that collagen is comprised of amino acids. The strands wind around one another in an alpha-helix. The quaternary structure of collagen consists of three left-handed helices twisted into a right-handed coil. The collagen (mainly type II), acts to constrain the proteoglycans and helps it hold its structure. ... disorders of the connective tissue could result also from defects Collagen and its disorders - SlideShare It is made of 66% to 86% water with the remainder consisting of primarily type II collagen (it may also contain type VI, IX, and XI) and proteoglycans. Chondrocytes organize the collagen, proteoglycans and non-collagenous proteins into a unique and highly specialized tissue, suitable for carrying out the functions stated above. One of the most noticeable functions of collagen is the support it provides for your skin. Collagen structure and function Collagen is the most abundant protein in the human body, accounting for around 30% of the total amount of protein. Structure of proteoglycans. Proline and hydroxyproline lack free amino (―NH 2) groups because the amino group is enclosed in a ring structure with the side chain; they thus cannot exist in a zwitterion form.Although the nitrogen-containing group (>NH) of these amino acids … The repeating sequence used to generate this model is Gly-Pro-Hyp. All collagens are composed of 3 polypeptide alpha chains coiled around each other to form the tripe helix configuration. Structure Bone architecture is made up of two types of bone tissue: l Cortical bone; l Cancellous bone. 4.10): The individual collagen polypeptide chains are first synthesised on membrane-bound ribosomes and then exported into the lumen of endoplasmic reticulum as larger precursor called the pro a-chain. Proteins: Structure and Functions By: Jamaica F. Tamayo f instrumental in about everything that Made up of chains of amino acids an organism does. • Foreign bodies left in the wound. Pyrrolidine ring Organic ring structure containing one atom of nitrogen; linkage to another amino acid through this • Chronic inflammation leads to excess, disabling fibrosis as in rheumatoid arthritis, pulmonary fibrosis and cirrhosis. Collagen molecules are linked to each other by covalent bonds building collagen ﬁbrils. A diagram of a collagen molecule. Collagen is composed of 3 chains. Also, they are widely spaced cells and their matrix is concentric in onion-like layers. The skin is divided into several layers, as shown in Fig 1. He was the first to propo… Hb binds O2 transports O2 and delivers the same to tissues. Type IV collagen is the main structural component of the basement membrane. This is important as this structural rearrangement defines hemoglobins oxygen-binding behavior. J Histochem Cytochem. Structure and function of arteries, capillaries and veins. Deregulation of ECM composition and structure is associated with the development and progression of several pathologic conditions. Most animal cells release materials into the extracellular space, creating a complex meshwork of proteins and carbohydrates called the extracellular matrix ( ECM ). Both have a-helix polypeptide chains that have a well-deﬁned amino acid sequence. Quaternary Structure Collagen is composed of a repeating Gly – X – Y sequence the X position is typically Pro and the Y position is often hydroxyproline allows three collagen polypeptides to wrap around one another forming a right-handed triple helix each polypeptide is helical with n=3.3 and a pitch of 10.0 Å Gly required at every 3rd Primary structure of protein means the order of amino acids. Collagen is the most common fibrous protein in the ECM, and it isi important for resisting tensile forces. Figure 7-14 Structure of collagen. Another protein found in the dermis, elastin, keeps skin flexible. The epidermis is composed mainly of keratinocytes. Depending on the primary function and the requirement of strength of the tissue the diameter of collagen ﬁbrils varies (the order of magnitude is 1.5 nm [17]). Based on the chemical nature, structure, shape and solubility, proteins are classified as: Simple proteins: They are composed of only amino acid residue. Fold classification databases give detailed information on the domain content of each protein and the fold associated with the domains. Collagen– most abundant protein in mammals. Identify the structure that is enclosed by the brackets in this electron micrograph. The GAGs extend perpendicular from the core protein in a bottlebrush- like structure. The organization at this level can actually be divided into four zones: 1) the superficial … Has collagen and elastin: Collagen is a protein that makes skin cells strong and resilient. Identify the tissue type and a location where it is found. In the next level of structure, called the microstructure between .0001 mm (.1 microns) and .1 mm (100 microns), we see the existence of the structural features of articular cartilage including the chondrocytes (cells that make cartilage matrix) and the organization of the type II collagen fibrils.
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