Answer:
The correct answer is option C.
Explanation:
As the proteins are produced in the endoplasmic reticulum membrane, they amalgamate with the vesicles and then they are conducted towards the membrane's cell surface where they act as an integral membrane protein.
The outer end will bind with the ligand and the other one will get attached towards the cytoplasm. Thus, the pinsulin in the given case will combine with the C terminus of the protein.
Answer:
1. transcription of Tau DNA in different directions.
4. different chemical modifications of Tau protein.
Explanation:
Tau gene transcribe in different direction which depends upon the animal age. This happens because at different age and developmental stage, animal produce different RNA binding proteins which leads to formation of alternative splice forms. This reaction is strengthen by the addition of phosphate and sugar molecules which again depending on developmental stage and time.
Cells because most living things like plant life and humans are made up of cells and animals are made up of cells too!
Phospholipids are typically made up of two fatty acids,a glycerol molecule and a phosphate group that is modified by an alcohol.The phosphate group is negatively charged, it is hydrophilic and it is describes as the polar HEAD of the phospholipid. The fatty acid chains have no charge [neutral], they are hydophobic and they are describe as the non-polar TAIL of the phospholipid.
Answer:
How do proteins adopt and maintain a stable folded structure? What features of the protein amino acid sequence determine the stability of the folded structure?
Proteins are formed by three-dimensional structures (twisted, folded or rolled over themselves) determined by the sequence of amino acids which are linked by peptide bonds. Among these bonds, what determines the most stable conformation of proteins is their tendency to maintain a native conformation, which are stabilized by chemical interactions such as: disulfide bonds, H bonds, ionic bonds and hydrophobic interactions.
How does disruption of that structure lead to protein deposition diseases such as amyloidosis, Alzheimer's disease, and Parkinson's disease?
The accumulation of poorly folded proteins can cause amyloid diseases, a group of several common diseases, including Alzheimer's disease and Parkinson's disease. As the human being ages, the balance of protein synthesis, folding and degradation is disturbed, which causes the accumulation of poorly folded proteins in aggregates, which can manifest itself in the nervous system and in peripheral tissues. The genes and protein products involved in these diseases are called amyloidogenic and all of these diseases have in common the expression of a protein outside its normal context. In all these diseases, protein aggregation can be caused by mere chance, by protein hyperphosphorylation, by mutations that make the protein unstable, or by an unregulated or pathological increase in the concentration of some of these proteins between cells. These imbalances in concentration can be caused by mutations of the amyloidogenic genes, changes in the amino acid sequence of the protein or by deficiencies in the proteasome.
Explanation:
