Answer:
Two members of the excavate clade that can cause disease are <u><em>diplomonads and parabasalids</em></u>
Explanation:
The excavate clade comprises of unicellular organisms which are eukaryotic. This group contains free-living organisms as well as organisms which form symbiotic relationships.
The diplomonads can be described as a group of flagellates which are considered to be parasitic. Some of them are even parasites to the humans.
The parabasalids are a group of flagellated protists within the supergroup Excavata. These organisms also form parasitic relationships.
3. A boat is moved forward by a current
4. The micronucleus
5. Alternation of generations
6. A. They are eaten by some whales
7. B. Oxygen is removed from the ocean by decomposition
The correct answer is the marble would weather more rapidly.
The weathering of the rock can be defined as the procedure of the erosion of the rock by various agents. The marble is a metamorphic form of the limestone. The limestone is easily affected by the hot and the humid climates. The rain and the atmospheric carbon dioxide get mix together form mild acids, this acid react with the limestone and causes the chemical changes. As a result, the marble is subjected to erosion in hot and humid climate.
In DNA there are two types of strands, 5'/5 prime, which is the strand, aka the leading strand.
There is also the 3' strand which is the lagging strand.
The difference between these two is the the leading strand is discontinous during replication, they must create ozaki fragments.
The other lagging strand can just have the whole strand replicated at the same time
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:
