•Describe the basic structure of collagen monomers •Explain how amino acid composition of collagen contributes to structure and Explain how collagen fibrils, fibers and sheets are formed and how that relates to their function.
A collagen monomer is a triple helix of three polypeptides. Two polypeptides are similar called alpha 1 and another differs slightly in aminoacid composition called alpha 2 .Each polypeptide is a left handed helix. The three left handed helices are twisted together in to a right handed triple helix (super helix). The super helix is stabilized by number of intrachain H-bonds.
Every third aminoacid in polypeptide is glycine. It also has proline and hydroxyproline contents.High glycine content will stabilize the collagen as it allows very close association of the collagen molecules with one another. Glycine is a very small aminoacid. Close association of collagen fibrils helps in H-bonding and other intermolecular association. In the triple helix, glycine is always placed in the center as it is small ans fits in the small place at the center. The H-bonds between glycine also help in keeping firm and stabilizing the triple helix .
Many collagen monomers bond to form fibrils by covalent cross linkings. Many collagen fibrils form collagen fibers. Number of collagen fibers give rise sheets. Sheets are used to cover different organs such as muscles, collagen fibers are seen in tendons, skin. Tendons are threads joining the muscle to bone which requires strength for attachment. As the collagen fibers are very rigid, they provide proper strength for attachment.
•Describe the basic structure of collagen monomers •Explain how amino acid composition of collagen contributes to...
describe the basic structure of an amino acid. what classes of amino acids are there?
Explain how/why the amino acid glycine and proline significantly impact the evolution of protein structure and function.
7.Draw the basic structure of an amino acid dimer (two amino acids bound together); label an amine, carboxyl, side chainand peptide bond. 8.Define primary and tertiary protein structure. How does the tertiary structure depend on the primary structure?
* 2.1 Describe different ways to classify amino acids and predict whether change in amino acid is likely to disrupt protein structure * 2.2 Compare and contrast the different levels of protein structure and how they relate to one another * 2.3 Describe the biochemical information that determines the final three-dimensional structure and explain what powers the formation of this structure * 2.4 Explain how structure determines function in general and using hemoglobin and myoglobin as specific examples. * 2.5...
How are organisms biologically organized? Describe the anatomy of the eukaryotic cell (animal and plant). Major difference between eukaryotes and prokaryotes. Describe the different types of chemical bonds. How do they affect the organization of biomacromolecules? Differentiate between a peptide bond, a phosphodiester, a phosphoanhydride bond. What are disulfide bridges? Amino-acids participating in this bonding? Describe the function of enzymes. Understand the forces by which substrates bind to enzymes. Distinguish between redox reactions and activated energy carriers. Distinguish between anabolism...
In the table below, describe the composition
and macromolecule structure for each of the
extracellular or cell interaction components. Do not include
specific amino acids or monosaccharides. Also, describe the
function(s) of each cell component.
Computer typed, please.
CATEGORY WHAT ARE THE GENERAL COMPOSITIONS AND STRUCTURES? WHAT ARE THE FUNCTIONS? Bacterial cell walls Plant cell walls Extracellular matrix Structural proteins Structural polysaccharides Adhesion proteins No composition needed here. Describe structure only. Integrins
1. Contrast the structure and function of myoglobin and hemoglobin. Describe the primary, secondary, tertiary and quaternary structure of both proteins. Describe their motifs and domains if appropriate. 2. How similar are the mammalian hemoglobin and myoglobin (in terms of amino acid composition)? 3. Recall the functions and structure of leghemoglobins, chlorocruorins, hemerythrin and hemocyanin. In what organisms are those proteins found? How are this globins different from mammalian globins? 4. Not all O2 molecules bind to each of the...
Justify with structure why arginine (pI=) is a more basic amino acid than histidine (pI=) is.
For each word define the word, describe molecular structure/composition/character, activity/catalysis, location within cells and how it contributes to cell or organisms functioning. a. Human SHOX gene b. Human SRY gene c. Genome
Describe the four categories of amino acid side chains. What types of interactions are the members of each of these categories likely to make? Now describe and explain the four levels of protein structure, giving a specific example of each an how amino acids are involved.