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Which type of bond is not typically involved in maintaining tertiary structure?

Which of the following amino acids is the least likely to be found in the interior of a globular protein?

A peptide bond is an example of which type of interaction?

Which situation below would most weaken a hydrogen bond between two molecules?

Which amino acid has a side chain that, due to its small size and lack of chirality, introduces conformational flexibility in protein loops?

A salt bridge in a protein structure is best described as:

Which of the following functional groups typically behaves as an electrophile in organic reactions?

The following is an excerpt from a recent scientific publication:“Covalent inhibitors can achieve exquisite potency and durable target occupancy through a combination of covalent and noncovalent interactions. Drugs that possess a covalent mechanism‑of‑action encompass recent blockbusters (Clopidogrel) as well as early cornerstones of modern medicine (aspirin and penicillin). Despite this well‑documented history and the advantages from sustained target engagement, pharmaceutical companies have traditionally shied away from covalent drug programs due to concerns about potential idiosyncratic toxicity. However, clinical successes over the past decade (e.g. Ibrutinib), along with improvements in technologies used throughout the drug discovery pipeline, have reignited broad interest in this class of therapeutics.” What key advantage of covalent inhibitors is emphasized here in drug discovery?

Which amino acid side chain is best suited to anchor a transmembrane helix in a lipid bilayer via hydrophobic interactions?

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