“how fast do hummingbirds fly? ” why is the question a scientific question?

4.06 hc)a five-year review of threats to the southern resident orca population of the united states concluded that the top threats were prey availability, contaminants, and effects from recreational and whale watching vessels. further down the list are oil spills, disease, and effects from commercial vessels not targeting whales. how might this list be different if it were for transient whale populations, which have a larger average population size and live farther offshore in open waters? a)the transient population is more likely to be affected by contaminants. b)the transient population is less likely to be affected by whale watching vessels. c)the transient population is more likely to be affected by disease. d)the transient population is less likely to be affected by prey availability.

Asmall number of finches are removed randomly from the wild and placed in a protected bird area. they are given as much food as they need and have plenty of space. why would natural selection not occur in this population? a. there is no reason for genetic mutation to occur. b. the birds compete for limited resources, c. the population has not reached carrying capacity. d. there is no genetic variation in the finches.

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