The following is an excerpt from a recent scientific publication:”…illustrating an internal H‑bond sampled between the piperidine and secondary amine nitrogen atoms… Internal H‑bond observed for the isolated compound becomes less likely in the presence of waters.” What inference can be made about oliceridine’s intramolecular hydrogen bonding in physiological (aqueous) environment?

What is the dominant type of noncovalent interaction between the side chains of phenylalanine and tryptophan in a folded protein?

Which amino acid has a bulky, hydrophobic, aromatic side chain that plays a major role in protein-protein stacking interactions?

In a globular protein, which of the following amino acids is most likely found on the exterior surface interacting with water?

Which amino acid side chain is most likely to participate in metal ion coordination in metalloproteins due to its lone pair donor properties?

Which of the following amino acids can simultaneously engage in ionic interactions and hydrogen bonding due to its guanidinium group?

Which amino acid’s side chain contains a nonpolar thioether group?

Which functional group contains a nitrogen atom bonded to three other atoms?

Which structural feature most directly explains cooperativity in hemoglobin but not in myoglobin?

Which of the following statements is true regarding covalent bonding in molecules?