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?

The following is an excerpt from a recent scientific publication:“In this study, we adopted the fragment‑based drug design approach … to extract noncovalent and covalent fragments according to distinct 3D interaction modes … we recombined BTK‑focused libraries, and 23 compounds within our libraries have been validated … provides valuable resources for virtual screening of covalent and noncovalent drugs targeting similar molecular targets.” For a kinase target like BTK, what is the advantage of combining covalent and noncovalent fragments in library design?

A molecule that contains a phenyl group has what type of functional group?

The following is an excerpt from a recent scientific publication:“From a chemical point of view, proteins are by far the most structurally complex… structure and chemistry… developed and fine‑tuned over billions of years… location of each amino acid… determines its three‑dimensional shape…. precise shape … determines function.” What evolutionary rationale underlies protein structure–function specificity?