If large amounts of protein are found in the urine, the kidneys are one of the structures that could be damaged. The liver might also be damaged.
stick with daily nutritional amounts. you could drink protein/ whey drinks as well.
It could release radiation.
it could change the entire dna structure, and cause deformations
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.
Bacteria added to the berries would be missing a certain protein.
The sequence of nucleotides in DNA molecule is equivalent and is closely related to an amino acid sequence in the protein molecule. If for any reason the sequence of DNA nucleotides changes it will be reflected in amino acid sequence in the protein. Moreover, the correct sequence of amino acid in the protein will form the correct three-dimensional structure, or tertiary structure, that will confer the biological activity to protein. If a wrong amino acid is translated from a mutated gene in the DNA could change the spatial structure of the protein and therefore modify or erase its biological function.
It could change the type of protein that would be produced hence change the structure and function of that protein.
Knowing the sequence of nucleotides within a gene allows you to determine the specific amino acid sequence of the protein encoded by that gene with the most accuracy. This information is crucial for understanding the structure and function of the protein and its potential role in biological processes.
When a globular protein has its hydrogen bonds broken, it can become denatured. This disrupts its folded structure, causing it to lose its specific shape and potentially its function. This could be reversible or irreversible depending on the extent of damage to the protein.
Changing the primary structure (sequence of amino acids) of a protein can alter its overall function due to changes in the interactions between amino acids. Additionally, modifying the tertiary structure (folding) of a protein can affect its active sites and binding capabilities, consequently impacting its function. Lastly, altering the quaternary structure (arrangement of multiple protein subunits) can lead to changes in protein-protein interactions and overall protein function.
beads of different colors joined together on a piece of string
Ethylene diamine tetraacetic acid (EDTA) is used in protein isolation to chelate and bind divalent metal ions, such as calcium and magnesium, which could potentially degrade the protein structure and function. By sequestering these metal ions, EDTA helps to stabilize the protein structure during the isolation process, preventing protein denaturation and maintaining its biological activity. Additionally, EDTA can also inhibit metal-dependent proteases, further protecting the integrity of the isolated proteins.