Which of the following is a product of glycolysis? * A)oxygen gas
B)carbon dioxide
C)pyruvic acid
D)water

Suppose a scientist measures the amount of dna per cell of a particular diploid species at various stages of meiosis. she finds that the meiotic cells contain 3.7 pg , 7.3 pg , or 14.6 pg of dna. match each stage of the cell cycle to the corresponding amount of dna contained within a cell at that stage.

The phylogeny chart shows the evolution of camels. camelus is the modern-day camel. based on this chart, which three statements are true? ⭕ modern camels are more related to stenomylus than to eschatius. ⭕ stenomylous and modern camels do not share a common ancestor. ⭕ modern camels are more related to camelops than to aepycamelus. ⭕ pliauchenia and oxydactylus may share similar features. ⭕ procamelus and stenomylous may share similar features.

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