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short answer if the shape of a protein is changed it could change the function by the results in disruption of cell activity and possibly cell death.

Conformational change of a functional protein, also known as denaturation. Denaturation is a process in which proteins or nucleic acids lose their structure (tertiary and secondary structure) by application of some external stress or compound for example, treatment of proteins with strong acids or bases, high concentrations of inorganic salts, organic solvents (e.g., alcohol or chloroform), or heat. If proteins in a living cell are denatured, this results in disruption of cell activity and possibly cell death. Denatured proteins can exhibit a wide range of characteristics, from loss of solubility to communal aggregation. Communal aggregation is the phenomenon of aggregation of the hydrophobic proteins to come closer and form the bonding between them, so as to reduce the total area exposed to water.

Proteins are very long strands of amino acids linked together in specific sequences. A protein is created by ribosomes that "read" mRNA that is encoded by codons in the gene and assemble the requisite amino acid combination from the genetic instruction, in a process known as translation. The newly created protein strand then undergoes posttranslational modification, in which additional atoms or molecules are added, for example copper, zinc or iron. Once this post-translational modification process has been completed, the protein begins to fold (spontaneously, and sometimes with enzymatic assistance), curling up on itself so that hydrophobic elements of the protein are buried deep inside the structure and hydrophilic elements end up on the outside. The final shape of a protein determines how it interacts with its environment.

When a protein is denatured, the secondary and tertiary structures are altered but the peptide bonds between the amino acids are left intact. Since the structure of the protein determines its function, the protein can no longer perform its function once it has been denatured. Most biological proteins lose their biological function when denatured. For example, enzymes lose their activity, because the substrates can no longer bind to the active site, and because amino acid residues involved in stabilizing substrates' transition states are no longer positioned to be able to do so.

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What determines the different shapes and functions of proteins?

A protein's structure is determined by:- the amino acid sequences of its polypeptide chains;- hydrogen bonds between amino acids in polypeptides;- other bonds (e.g. hydrophobic interactions, disulphide bridges) between side chains in the polypeptides; and- the arrangement of polypeptides (in a protein that contains more than one polypeptide)Scientists have mapped the structures of several proteins; however, scientists are still unsure as to how proteins actually form their final structures.The function of a protein is directly related to its structure. For example, a protein that fights a certain bacteria might have a shape that allows it to bind to the bacteria and then destroy it.


If a mutation occurred during the formation of a protein that substituted an amino acid with a reactive R group for one that had a nonreactive R group how might this affect the reactivity?

A mutation is a change in DNA, so when u change the DNA this affects the sequence of the amino acid in the primary structure. this later changes the folding of the r groups because u don't have the right unique sequence of amino acid that was encoded by the DNA


What is the advantages of using biuret reaction in place of measuring the absorption of the protein solution at 280 nm?

The absorption of proteins at 280nm is according to electrons from the rings on the amino acid such as His, Trp, etc. And if there is no such kind of amino acids in the protein, we might not be able to get what the amount of the protein really is. At the other hand, what makes biuret reaction work is by the copper ion reacting with the dipeptide bonds, since every amino acid has the peptide bond, it's more accurate and reasonable to use biuret reactions to determine what the amount of the protein is.


What might be occurring on a molecular level during the rest periods?

During rest periods, molecular processes such as DNA repair, protein synthesis, and energy storage may be occurring. Cells might be replenishing energy stores, repairing damaged molecules, and synthesizing new proteins to support cellular functions. This allows the body to recover and prepare for the next activity.


What is the difference between polypeptide and protein?

First, it is important to know that all proteins are technically polypeptides, although in general scientists consider polypeptides molecules consisting of one strand of amino acids chemically bound to one another that have no special or unique properties. It would be very difficult or impossible to find a degreed and professional scientist who considers all polypeptides proteins. One difference between what is called a "polypeptide" and a "protein" is based on the number of amino acids each one contains. A chain of amino acids that contains relatively few amino acids compared to known proteins is a "polypeptide." The second most important distinction between how the two words are used is that scientists normally reserve the word "protein" for molecules consisting entirely or nearly entirely of amino acids that exhibit specialized physical or chemical properties, or both. For example, hemoglobin is considered a "protein" because it is specialized to carry the oxygen in our red blood cells. Keratin is another protein that serves as a structural material in our skin and is the material of which hair is made. On the other hand aspartame, the artificial sweetener, is a polypeptide since it only consists of three amino acids chemically bound to one another, thus it is too small to be called a protein. I can see how one might argue that it is a protein because it has a powerful sweet taste, however there are several other chemical compounds that are not sugars that also have a powerful sweet taste. (What would otherwise be the carboxylic acid end of aspartame has been changed to its methyl ester.)

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