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.
A protein's function is directly tied to its specific shape. If the shape of the protein is changed, it may no longer be able to interact properly with other molecules it needs to function correctly. This can disrupt its ability to carry out its normal biological activities.
Enzymes are composed of proteins, and the thing to remember with pproteins is that they are very complex, and each structure of the protein (primary to quaternary) will determine the exact function. If there is a chance in shape, then the function of the enzyme will also change, so this would give rise the possibility of the enzyme not working.
because it would have different function
It's continuously processed in the nitrogen cycle. In broad outline nitrogen in the atmosphere is fixed by bacteria so that it's available to plants making protein. This protein is consumed by animals and plants or returned to the atmosphere as methane. The plant nitrogen is converted to animal protein which is eventually returned to the atmosphere by bacteria. For more detail you might wish to refer to information on wikipedia.
The sequence of amino acids in a protein determines its unique shape and function. This sequence is specified by the DNA sequence of the gene that encodes the protein. Through a process called protein folding, the amino acid chain folds into a specific three-dimensional shape that enables the protein to carry out its specific function.
Can the manufacturer, Reynolds, please answer this question. The material used for this diamond brand aluminium foil might not be pure aluminium.
The mutation could potentially increase the reactivity of the protein if the substituted amino acid with the reactive R group allows for new chemical reactions to occur. On the other hand, if the nonreactive R group is essential for the protein's normal function, the mutation could disrupt the protein's activity. Ultimately, the effect on reactivity would depend on the specific amino acids involved and the role they play in the protein's structure and function.
One advantage of using the biuret reaction is that it can measure total protein concentration, not just proteins that absorb at 280 nm like tryptophan and tyrosine containing proteins. Additionally, biuret assay is more sensitive and can detect a wider range of protein concentrations compared to absorbance at 280 nm.
There are multiple reasons for this. If you didn't log in to Poptropica for six months, it was deleted. You might have entered your username or password incorrectly. If someone had access to your password, they might have changed it. You might not match the system requirements needed to play Poptropica.
It will depend on how different the amino acid is to the one it replaced. If the structure and/or charge is quite different, a change of one amino acid can change the entire 3D structure of the protein. This will affect the proteins function.
The protein might be unable to function.
The protein might be unable to function.
It might have changed because the name changed
It might have changed because the name changed
Misperceive means to perceive incorrectly. I am afraid she might misperceive my intentions.
Mutant protein will form.
It might have changed because the name changed
Cyclin
One might drink whey protein shakes to help supplement their diet with additional protein. Whey protein is a very fast absorbing type of protein so it is very useful for building and repairing muscle tissue after weight training.
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