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Polysaccharide Shapes | D. A. Rees | Springer
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Because it has more ends, it can be broken more quickly than amylose by amylase enzymes. Glycogen is similar in structure to amylopectin. It is made by animals as their storage polysaccharide, and is found mainly in muscle and liver. Because it is so highly branched, it can be mobilised broken down to glucose for energy very quickly. Cellulose is only found in plants, where it is the main component of cell walls.
It is poly glucose, but with a different isomer of glucose. Starch and glycogen contain a-glucose, in which the hydroxyl group on carbon 1 sticks down from the ring, while cellulose contains b-glucose , in which the hydroxyl group on carbon 1 sticks up. This means that in a chain alternate glucose molecules are inverted.
Polysaccharide shapes and their interactions - some recent advances
This apparently tiny difference makes a huge difference in structure and properties. While the a glucose polymer in starch coils up to form granules, the b 14 glucose polymer in cellulose forms straight chains. Hundreds of these chains are linked together by hydrogen bonds to form cellulose microfibrils.
These microfibrils are very strong and rigid, and give strength to plant cells, and therefore to young plants and also to materials such as paper, cotton and sellotape. The b-glycosidic bond cannot be broken by amylase, but requires a specific cellulase enzyme.
The only organisms that possess a cellulase enzyme are bacteria, so herbivorous animals, like cows and termites whose diet is mainly cellulose, have mutualistic bacteria in their guts so that they can digest cellulose. Humans cannot digest cellulose, and it is referred to as fibre. Other polysaccharides that you may come across include: Chitin poly glucose amine , found in fungal cell walls and the exoskeletons of insects. Pectin poly galactose uronate , found in plant cell walls.
Agar poly galactose sulphate , found in algae and used to make agar plates. Murein a sugar-peptide polymer , found in bacterial cell walls. Lignin a complex polymer , found in the walls of xylem cells, is the main component of wood. They have an astonishing range of different functions, as this list shows. Proteins are made of amino acids. The general structure of an amino acid molecule is shown on the right.
There is a central carbon atom called the "alpha carbon" , with four different chemical groups attached to it:. At neutral pH found in most living organisms , the groups are ionised as shown above, so there is a positive charge at one end of the molecule and a negative charge at the other end. The overall net charge on the molecule is therefore zero. A molecule like this, with both positive and negative charges is called a zwitterion.
The charge on the amino acid changes with pH:. It is these changes in charge with pH that explain the effect of pH on enzymes. There are 20 different R groups, and so 20 different amino acids. Since each R group is slightly different, each amino acid has different properties, and this in turn means that proteins can have a wide range of properties. The following table shows the 20 different R groups, grouped by property, which gives an idea of the range of properties. You do not need to learn these, but it is interesting to see the different structures, and you should be familiar with the amino acid names.
You may already have heard of some, such as the food additive monosodium glutamate, which is simply the sodium salt of the amino acid glutamate. Be careful not to confuse the names of amino acids with those of bases in DNA, such as cysteine amino acid and cytosine base , threonine amino acid and thymine base.
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There are 3-letter and 1-letter abbreviations for each amino acid. Simple R groups. Basic R groups. Hydroxyl R groups. Acidic R groups. Sulphur R groups. Ringed R groups. Cyclic R group. Amino acids are joined together by peptide bonds.
Structure and Function of Carbohydrates
The reaction involves the formation of a molecule of water in another condensation polymerisation reaction:. When two amino acids join together a dipeptide is formed. Three amino acids form a tripeptide.
Many amino acids form a polypeptide. In a polypeptide there is always one end with a free amino NH 3 group, called the N-terminus , and one end with a free carboxyl CO 2 group, called the C-terminus. In a protein the polypeptide chain may be hundreds of amino acids long. Amino acid polymerisation to form polypeptides is part of protein synthesis.
It takes place in ribosomes, and is special because it requires an RNA template. The sequence of amino acids in a polypeptide chain is determined by the sequence of the genetic code in DNA. Protein synthesis it studied in detail in module 2. Polypeptides are just a string of amino acids, but they fold up to form the complex and well-defined three-dimensional structure of working proteins. To help to understand protein structure, it is broken down into four levels:. Primary Structure. This is just the sequence of amino acids in the polypeptide chain, so is not really a structure at all.
However, the primary structure does determine the rest of the protein structure. Finding the primary structure of a protein is called protein sequencing , and the first protein to be sequenced was the protein hormone insulin, by the Cambridge biochemist Fredrick Sanger, for which work he got the Nobel prize in Secondary Structure.
This is the most basic level of protein folding, and consists of a few basic motifs that are found in all proteins.
The secondary structure is held together by hydrogen bonds between the carboxyl groups and the amino groups in the polypeptide backbone. The two most common secondary structure motifs are the a -helix and the b -sheet. The a -helix. The polypeptide chain is wound round to form a helix. It is held together by hydrogen bonds running parallel with the long helical axis.
Polysaccharide Shapes (Paperback)
There are so many hydrogen bonds that this is a very stable and strong structure. Do not confuse the a-helix of proteins with the famous double helix of DNA. Helices are common structures throughout biology. The b -sheet. The polypeptide chain zig-zags back and forward forming a sheet of antiparallel strands.
Once again it is held together by hydrogen bonds. The a -helix and the b -sheet were discovered by Linus Pauling, for which work he got the Nobel prize in There are a number of other secondary structure motifs such as the b -bend, the triple helix only found in collagen , and the random coil. Tertiary Structure. This is the compact globular structure formed by the folding up of a whole polypeptide chain.
Every protein has a unique tertiary structure, which is responsible for its properties and function. For example the shape of the active site in an enzyme is due to its tertiary structure. The tertiary structure is held together by bonds between the R groups of the amino acids in the protein, and so depends on what the sequence of amino acids is. There are three kinds of bonds involved:. So the secondary structure is due to backbone interactions and is thus largely independent of primary sequence, while tertiary structure is due to side chain interactions and thus depends on the amino acid sequence.
Quaternary Structure. This structure is found in proteins containing more than one polypeptide chain, and simply means how the different polypeptide chains are arranged together. The individual polypeptide chains are usually globular, but can arrange themselves into a variety of quaternary shapes. Haemoglobin , the oxygen-carrying protein in red blood cells, consists of four globular subunits arranged in a tetrahedral pyramid structure. Each subunit contains one iron atom and can bind one molecule of oxygen.
Immunoglobulins , the proteins that make antibodies, comprise four polypeptide chains arranged in a Y-shape. The chains are held together by sulphur bridges. This shape allows antibodies to link antigens together, causing them to clump. Actin , one of the proteins found in muscles, consists of many globular subunits arranged in a double helix to form long filaments. Tubulin is a globular protein that polymerises to form hollow tubes called microtubules.
Carbohydrase enzymes are produced in your mouth in saliva , pancreas and small intestine. Proteins are large molecules made from amino acids joined together to form chains. They include enzymes , haemoglobin , collagen and keratin. Each protein has hundreds, or even thousands, of amino acids joined together in a unique sequence and folded into the correct shape. This gives each protein its own individual properties. Protease enzymes are responsible for breaking down proteins in our food into amino acids. Then different enzymes join amino acids together to form new proteins needed by the body for growth and repair.
Protease enzymes are produced in your stomach, pancreas and small intestine.