An artificial membrane separates two sides of a beaker. The left side contains 50 glucose molecules and the right side contains 100 fructose molecules. If you add channels to the membrane for glucose molecules but do not add any for fructose molecules and then wait for a while, which will more likely be true? A. The 50 glucose molecules will have moved from the left side to the right side of the beaker, because the channels allowed them to cross the membrane.
B. The 50 glucose molecules will not have moved to the right side of the beaker, because there are already 100 fructose molecules on the right side of the beaker.
C. About 25 glucose molecules will be on the right side of the beaker, and 25 will be on the left side of the beaker.
D. Both sides of the beaker will contain approximately equal numbers of glucose and fructose molecules.

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