Question Completion with Options:
a. increasing the size of your cohorts.
b. increasing the diversity of your cohorts.
c. increasing the size of your affected cohort.
d. increasing the diversity of your affected cohort.
Answer:
All of the following modifications to the study are likely to allow identification of new variants associated with the disease, EXCEPT
a. increasing the size of your cohorts.
Explanation:
Option A is chosen because increasing the size of the cohorts will be equally divided between the affected and unaffected cohorts since the study discovered that these two classes are roughly the same size. Therefore, new variants of the disease may not likely be identified and isolated unless the other modification options are followed instead of Option A.
The answer to the question is D
Answer:
the capitol is Washington DC
Answer;
-On the polar end or the hydrophillic end of the protein.
Explanation;
-Each amino acid has at least one amine and one acid functional group as the name implies. The different properties result from variations in the structures of different R groups.The R group is often referred to as the amino acid side chain.
-Side chains which have various functional groups such as acids, amides, alcohols, and Amines will impart a more polar character to the amino acid. Polar amino acids include serine, threonine, asparagine, glutamine, histidine and tyrosine.
Therefore; serine being a polar or hydrophillic amino acid will be found on the polar side chain of the protein.
Answer:
The correct answer is myofibrils
Explanation:
The fundamental part of the muscle cytoskeleton is made up of myofibrils that are the contractile elements of skeletal muscle cells.Muscle fibers are made up of myofibrils, membranes, and cytoskeletal networks that anchor contractile fibrils to the sarcolemma. Myofibrils are composed of repeating contractile units known as sarcomeres and are perhaps the most ordered macromolecular structures in eukaryotic cells. Myofibrils are made up of actin and myosin filaments that are large polymerized protein molecules responsible for actual muscle contraction.
