Proteins And Functions Of Proteins Essay

3. State the name and structure of the functional group for each type of biologically

gluconeogenesis slow down in which release of glucose to the blood stream is also slowed down

Coelomates have an enclosed body cavity, which means advance muscle structure, enhanced locomotor capabilities, and more structural integrity.

A chemical reaction involving the transfer of electrons rather than molecules is classified as a Redox reaction. A reaction involving the loss of electrons is called Oxidation, and a reaction involving the gain of electrons is called Reduction. Oxidation and Reduction always occur together, as one reactant loses electrons, and the other gains them. This exchange often effects the physical states of molecules, as their solubility is changed with their charge.

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sHSPs are a ubiquitous class of chaperones found across all kingdoms of life. sHSP range in size from 12-42 kilo Daltons in large oligomers of 12 to >32 subunits and the structure is homologous across all species. The sHSP monomer consists of three domains: a disordered N-terminal arm, a beta-sandwich α-crystallin domain, and a flexible C-terminal extension. The N-terminal domain is the most variable region with little conservation between species. Experimental evidence also suggests N-terminal involvement in substrate binding and protection. The α-crystallin domain is the most highly conserved region and adopts a β-sandwich conformation composed of 7 to 8 anti-parallel β-strands (Basha et al, 2012). The C-terminus contains an I-X-I motif, which helps to satblizie the oligomeric form of the sHSP (Basha et al, 2012).

The objective of the lab was to identify numerous macromolecules in 12 pre-chosen chemicals. To carry out the lab, three different tests were performed: The Iodine test, Benedict’s test and Biuret test. The twelve chemicals that were being tested on throughout the experiment included: 1% glucose solution, 0.3% glucose-1-phosphate, 1% maltose sugar, honey solution, 1% sucrose solution, 1% lactose solution, 1% glycogen solution, 1% starch solution, protein, beer, distilled water and an unknown substance “unknown 193”.

Proteins are polymeric chains that are built from monomers called amino acids. All structural and functional properties of proteins derive from the chemical properties of the polypeptide chain. There are four levels of protein structural organization: primary, secondary, tertiary, and quaternary. Primary structure is defined as the linear sequence of amino acids in a polypeptide chain. The secondary structure refers to certain regular geometric figures of the chain. Tertiary structure results from long-range contacts within the chain. The quaternary structure is the organization of protein subunits, or two or more independent polypeptide chains.

Amino acid can be found in food we eat every day for example it can be found in meat and dairy. It is extremely common in meat such as pork,beef and chicken. It is also common in dairy products such as eggs,milk,yogurt and cheese. Both meat and dairy contain protein as amino acid is one of the key components that make up protein. Protein is made up of hundreds of small compounds, one of which is amino acids. They all attach into long chain by something called peptide bonds and all of these long chains join together and form protein which is in the foods we eat and is an essential compound in the body.

The effects of integrin’s vary from the type of protein they are and how they affect a certain part of the body. They are usually surface receptors that will interact with extracellular matrix. There is a family of alpha and beta classes which would usually form heterodimers. They are used for adhesion purposes most of the time and can also transduce a biochemical signal into or out of the cell. This process is called bidirectional, where the can transmit information from in and out of a cell. There are different structures that integrin’s play a role in. Integrin’s can bind to a ligand, where it will form a complex with a biological molecule that will usually serve as a purpose. They can go through a process called activation, where they would have a conformational change of the receptor. They can also trigger a cascade effect, which can change a receptors shape.

Although approximately 42 dominant SCAs have been identified only 20 have been genetically identified. Most of the identified SCAs share a common mutation: SCA1 SCA2, SCA 3, SCA6, SCA7, SCA8, SCA12, SCA17 have all been linked to the same CAG trinucleotide repeat but in different varying chromosomes and loci. These are also known as polyglutamine (Poly-Q) diseases. Poly-Q proteins are extended proteins formed by an expansion of the mRNA that coded for the amino acid chain during translation. The Polyglutamine-expansion disease family encompasses at least nine heritable disorders, including Huntington disease (HD) and the spinocerebellar ataxias SCA1, SCA2, SCA3, SCA6, SCA7 and SCA17. 11 Normally the proteins formed

Bettelheim, Brown, Campbell and Farrell assert that polypeptide chains do not extend in straight lines but rather they fold in various ways and give rise to a large number of three-dimensional structures (594). This folding or conformation of amino acids in the localized regions of the polypeptide chains defines the secondary structure of proteins. The main force responsible for the secondary structure is the non-covalent

Immunoglobulin (Ig) or Antibody (AB) is a protein that is in the shape of a Y that is produced by plasma cells and use by the immune system. These proteins are then utilized to identify and attack bacteria and viruses. Immunoglobulin is clearly a very important protein in our human bodies as well as being very integral to our survival and our ability to fend off foreign molecules. This has lead to a lot of deep research regarding this protein. By knowing the proteins exact structure and functions there will be a larger understanding of how our bodies actually work and how we can improve our health to live longer and better lives. This is exactly what will be looked at throughout this paper, the research, structure, function and behavior of the protein Immunoglobulin (Ig).

The Functions of Proteins Introduction Protein accounts for about three-fourths of the dry matter in human tissues other than fat and bone. It is a major structural component of hair, skin, nails, connective tissues, and body organs. It is required for practically every essential function in the body. Proteins are made from the following elements; carbon, hydrogen, oxygen, nitrogen and often sulphur and phosphorus.

Enzymes are an important part of all metabolic reactions in the body. They are catalytic proteins, able to increase the rate of a reaction, without being consumed in the process of doing so (Campbell 96). This allows the enzyme to be used again in another reaction. Enzymes speed up reactions by lowering the activation energy, the energy needed to break the chemical bonds between reactants allowing them to combine with other substances and form products (Campbell 100). In this experiment the enzyme used was acid phosphates (ACP), and the substrate was p-nitrophenyl phosphate.