A researcher found that the wild species of almond trees contains a chemical called amygdalin. This chemical is converted into cyanide inside the human body and can be lethal. The researcher found that a single gene mutation in some of the wild almond trees resulted in a variety that no longer produced the chemical amygdalin. This variety of almond is largely
harvested for human consumption. Based on the study, the researcher claimed that some mutations are beneficial in nature.
Was the claim made by the researcher correct?
•Yes. The mutated variety of almonds was edible.
•No. Not all almond trees produced seeds that were edible.
•No. The mutation did not affect all varieties of almond trees.
•Yes. Almond trees with amygdalin grew only in forests.

The gene that causes sickle-cell disease is present in a higher percentage of residents of sub-saharan africa than among those of african descent living in the united states. even though this gene causes sickle-cell disease, it also provides some protection from malaria, a serious disease that is widespread in sub-saharan africa but absent in the united states. discuss an evolutionary process that could account for the different percentages of the sickle-cell gene among residents of the two regions.

Surrounded by microtubules, located near the nucleus. (don't try to google it) (give answer only if u know)

Match the descriptions / definitions with the term they best describe 1. three dimensional relationship of the different polypeptide chains in a multisubunit protein or protein complex 2. common folding pattern in proteins in which a linear sequence of amino acids folds into a right-handed coil stabilized by internal hydrogen-bonding between polypeptide backbone atoms. 3. the amino acid sequence of a protein 4. a region on the surface of a protein that can interact with another molecule through noncovalent bonding. 5. three-dimensional arrangement of alpha-helices and beta-sheets within a single polypeptide, typically stabilized by a variety of noncovalent bonds, including ionic and hydrogen bonds, and nonpolar interactions / hydrophobic force. 6. the chain of repeating carbon and nitrogen atoms, linked by peptide bonds, in a protein. 7. common structural motif in proteins in which different sections of the polypeptide chain run alongside each other and are joined together by hydrogen bonding between atoms of the polypeptide backbone. 8. portion of a polypeptide chain that has a discrete tertiary structure of its own and can often fold independently of the rest of the chain 9. regular local folding patterns in a protein, including alpha-helix and beta-sheet a. primary structure b. beta-sheet c. protein d. coiled-coil e. polypeptide backbone f. secondary structure g. side chain h. tertiary structure i. binding site j. alpha-helix k. quaternary structure l. protein domain