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Complex Macromolecules: The Five Types Of Proteins

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Proteins are complex macromolecules that are formed by elements carbon, hydrogen, oxygen and nitrogen. Proteins composed of one or more polypeptide chains of amino acids. The main functions of proteins are to structure, support, protect, make movement, catalyst, transport and make hormones in human body. In the structural role, collagen and elastin provide support for connective tissue. Actin and myosin are proteins that involved in muscle contraction and movement. Haemoglobin is a protein that transports oxygen through the blood. For protection, there are immunoglobulins. Immunoglobins are glycoprotein molecules that are produced by plasma cells. It functions as antibodies. There are five types of immunoglobulins, which is IgG, IgA, IgM, IgD, and IgE. They are many different functions for each of the immunoglobulins. …show more content…

Amino acids are the building blocks of proteins. All amino acids have the same basic structure but differ in their R-side chains. Each amino acid consists of an amino group (-NH3), a carboxyl group (-COOH) and a hydrogen atom (H). The amino and carboxyl groups are attached to a central alpha carbon together with a hydrogen atom and an R-side chain. There are currently known that over 170 amino acids occur in organisms but only 20 are commonly found in proteins. R groups determine the chemical properties of the amino acids. The simplest amino acids have hydrocarbons as side chains which are neutral and non-polar or hydrophobic. They are not soluble in water. Amino acids with a polar R group are neutral and polar or hydrophilic. They are more soluble in water. Polar side chains can be uncharged or carry a negative or positive

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All enzymes are under the class of protein biomolecule. Amino acids are the basic units that are combined to make up an enzyme. The biomolecule that stores information is a Nucleic Acid. The specific 3-D region within an enzyme is called the active site. The chemical

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Each amino acid is made up of an amino group, a carboxyl group and a side chain (Reece, J. B., Urry, L. (2016). Campbell biology. Boston Pearson). Enzymes work by lowering the activation energy of the reaction making the reaction produce faster. Enzymes begin to catalyze chemical reactions with the binding of the substrate to the active site on the enzyme.

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It was clear that the hemoglobin molecules of individuals with sickle cell anemia migrated at a different rate, and thus ended up at a different place on the gel, from the hemoglobin of normal individuals. Individuals with sickle cell trait had about half normal and half sickle cell hemoglobin, each type making up half of the contents of the heme groups in any red blood cell. Substitution mutations that result in the replacement of one amino acid by another with a different electrical charge can lead to changes in the overall charges of the protein. Amino acids consist of an amino and a carboxyl group bound to the same carbon atom and a side chain that specifies for the 20 different amino acids present in our proteins. Amino or carboxyl groups in the side chain make the amino acid either basic or acidic.

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A: Phospholipid A1: Phosphate head (hydrophilic, polar) A2: Two fatty acid tails (hydrophobic, non-polar) B: Glycolipid C: Glycoprotein D: Carbohydrate E: Cholesterol F: Integral Membrane Protein G: Channel Protein H-I: Phospholipid Bi-layer (b) Explain how the properties of molecules A and C cause them to be arranged as shown in the plasma membrane.

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Hemoglobin is made out of two alpha and two beta polypeptide chains and heme bunches; each containing a focal particle of iron. At the point when the iron is in the diminished shape and not appended to oxygen, the hemoglobin is called deoxyhemoglobin, or decreased hemoglobin; when it is connected to oxygen, it is called oxyhemoglobin. Deoxyhemoglobin joins with oxygen in the lungs (the stacking response) and breaks its bonds with oxygen in the tissue capillaries. A. Very still, the distinction in the middle of blood vessel and venous oxyhemoglobin immersions shows that around 22% of the oxyhemoglobin dumps its oxygen to the tissues. Amid exercise, the venous PO2 and percent oxyhemoglobin immersion are diminished; showing a higher percent of

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Protein is needed by the body for a variety of functions, such as wound healing, muscle building and immune function. Red meat is also a good source of iron, which is needed for red blood cell production. These amino acids are good for helping build

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During, Cell Structures Involved in Cell Transport discusses the plasma membrane and its role. The plasma membrane consists of a phospholipid bilayer arranged back – to – back. The phospholipid bilayer contains membrane proteins that perform various functions. These membrane proteins are integral protein, peripheral protein, transport protein, carrier protein, ion channel protein, channel protein and gated channel protein. The membrane is selectively permeable which certain molecules are allowed to enter and exit the cell.

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1) Amide is the most polar of the functional groups. The reason is that it can make hydrogen bond and accept hydrogen bonds on both the oxygen and the nitrogen. Acid would be the second most polar as the hydrogen bonding capabilities and the presence of two oxygen atoms b) Ether would be on of the most non-polar because the lack of any oxygen-hydrogen bond makes hydrogen bonding impossible. There is little intermolecular association Ethers are essentially non-polar and insoluble in water. Hydrocarbon is also one of the most non-polar since there is little intermolecular association because the carbon-hydrogen bond is non-polar.

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has a slight higher affinity for oxygen than haemoglobin, especially at lower layers. This is because myoglobin has an easier job in that it only needs to store oxygen and release it for the muscles, while haemoglobin also has to transport the oxygen and release it in the correct areas. Haemoglobin is formed in the body by DNA just like all the other proteins. Alterations or mutations to haemoglobin causes many blood related diseases such as sickle-cell anaemia. Where the cell structure is coloured and can no longer hold as much oxygen in the right way as a normal blood cell.

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Proteins play a very important role in the human body. Our everyday lives are dependent on proteins functioning correctly. The human body contains many many proteins that must all work together perfectly or problems can occur. There are several different types of proteins also in the human body, but the one being focused on will be the Calcium Pump protein, which is located in mainly muscle cells (Klabunde, 2010). The calcium pump works by pumping calcium out of the cell (Klabunde, 2010).

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Proteins are complex molecules made of amino acids that perform important functions for everyday living such as controlling the activity of genes in DNA. Recommended daily amounts by the United States Department of Agriculture are shown in the table below. These protein recommendations are appropriate for individuals who are moderately active. Children 2-3 years old 4-8 years old 2 ounce equivalents 4 ounce equivalents Girls 9-13 years

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The amino acid glutamate normally contains a single negatively charged COO-, or carboxylic acid group in its side chain. An additional COO- group allows glutamate to bind positively charged calcium ions much more effectively. Vitamin K is an essential cofactor in the enzymatic reaction producing gamma

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Proteins are made up of peptide bonds holding amino acids together to perform biological functions like enzymes, antibodies, for transport and structure (Asmus, 2007). Lastly, nucleic acids

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they contain all the essential amino acids and enough of them to build new tissue. Chief sources include meat, milk, fish, and eggs i.e. animal foods. This is because animal protein resembles the amino content of human tissue. Low biological value proteins come from plant sources. They don’t contain enough amino acids to build tissue.

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A group of 3 nucleotides is called codons. Each codon on the mRNA molecule matches a corresponding anti-codon on the base of a tRNA molecule. The tRNA anti-codon attaches to the mRNA codon. Then, the larger subunit of the ribosome disconnects an amino acid from a corresponding tRNA molecule and adds it to the growing protein chain. When the mRNA is completely decoded a protein is made

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