pat

Ok, so far, for the H-bonds, i'm showing Leu-C=0---H-O-Tyr of a another protein, which shows that Hydrogen is interacting with another electronegative element. I also have the ionic interaction finished in a similar fashion, but i am stuck on the hydrophobic interaction. Don't know how to show that..

"A 100mL solution containing 1M sodium acetate was made. The pH was than adjusted to 5.5. A similar solution containing NaCl was also made and treated similarly. Then 1mL of 1M NaOH was added to both solutions. Qualitatively (no numbers/calculations are necessary) explain what if any difference in the change in pH occurs between the two solutions. If the pH changes in the two solutions are different, explain why. For both solutions, explain (draw) what is happening to all of the chemical entities (e.g molecules) in the solution with the NaOH?"----Any help would be great!!

"Draw an example of a functional group found in an enzyme that would act as a base. What part of the enzyme contains that functional group? Explain how/why it acts as a base?"-----Any help on this topic would be greatly appreciated!!!

"The major non-covalent forces related to the formation of protein structures are H-Bonds, ionic interactions(electrostatic interactions), and hydrophobic interactions(which are caused by things like Van der waals forces). Give (draw) examples of how the dipeptide (L-Asn-L-Leu) could participate in each one of those types of interactions with functional groups frequently found in proteins? Make it clear exactly what atom/group is interacting with what other atom/groups. Explain the interaction you have drawn and why they fit one of the three categories given? " --I know this is a mouthful but any help would be greatly appreciated!!