Scientists have noticed that the entire DNA molecule has the same width, despite the fact that the four nucleotides are NOT the same width Now that you’ve created a model, explain why this makes sense (hint: it has to do with the number of rings for each nitrogen base)

You have a solution that contains phospholipid vesicles in a test tube. these vesicles have phospholipid bilayers, but do not contain any membrane transporters. you add a number of different molecules to the solution, and wait a period of time for them to equilibrate. if you could measure the concentration of each molecule, for which of the following would you expect to measure equal concentrations inside and outside of the vesicles? assume for this question that the overall osmolarity inside and outside the vesicles is the same (that is, there is no appreciable diffusion of water across the membrane). (select two answers) an amino acid with a hydrophobic side-chain a small non-polar molecule a negatively charged ion a small polar molecule a small lipid hormone

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

Identify any four organelles that should be present in the eukaryotic organism and describe the function of each organelle