Human serum albumin (HSA) is the most abundant plasma protei…

Human serum albumin (HSA) is the most abundant plasma protein and a versatile carrier that transports a wide range of ligands. It binds long‑chain fatty acids at multiple high‑affinity sites located across distinct protein subdomains, using hydrophobic pockets and specific hydrogen‑bond/ionic interactions to stabilize the anionic carboxylate headgroups. By buffering and distributing fatty acids between tissues, HSA modulates their bioavailability, prevents micelle formation and toxicity in plasma, and delivers them to cells via reversible, concentration‑dependent binding. The figure below is an excerpt taken from a paper titled “Chain Length-dependent Binding of Fatty Acid Anions to Human Serum Albumin Studied by Site-directed Mutagenesis”, published in 2006 in the Journal of Molecular Biology. The graphs compare the binding of 4 different fatty acids of varying length (octanoate = 8 carbons, decanoate = 10 carbons, laurate = 12 carbons, myristate = 14 carbons in length) to the wildtype HSA and to a mutant HSA they created in the lab (denoted as R410A, which indicates that the amino acid at position 410 in the wildtype protein is normally an R but the researchers intentionally changed it to an A). Given these results, which of the following is an accurate statement?

Excerpts from the paper “Structure and evolution of the Ivy…

Excerpts from the paper “Structure and evolution of the Ivy protein family, unexpected lysozyme inhibitors in Gram-negative bacteria” are presented below. The Ivy–lysozyme interface shows high shape complementarity. Which substitution in Ivy would most plausibly reduce inhibitory potency by introducing steric clash without compensating interactions?

Human serum albumin has many natural genetic variants, but m…

Human serum albumin has many natural genetic variants, but most are rare. Their frequency differs by population; some detectable forms (like bisalbuminemia or certain named variants) appear roughly between about 1 in 1,000 to 1 in 3,000 people in some groups. These variants usually don’t cause disease, but they can slightly change how albumin binds molecules and are useful for studying human populations and protein function. The figure below is taken from a paper titled “Chain Length-dependent Binding of Fatty Acid Anions to Human Serum Albumin Studied by Site-directed Mutagenesis”, published in 2006 in the Journal of Molecular Biology. Considering this, choose all of the following statements that are correct.

The information below is an excerpt from a 2025 publication…

The information below is an excerpt from a 2025 publication in Nature titled “Structural and functional characterization of human sweet taste receptor”. Certain T1R2 VFT mutations shift EC50 values for multiple sugars in parallel. What structure–function conclusion is most consistent with this pattern?

Excerpts from the paper “Structure and evolution of the Ivy…

Excerpts from the paper “Structure and evolution of the Ivy protein family, unexpected lysozyme inhibitors in Gram-negative bacteria” are presented below. The Ivy–lysozyme interface shows high shape complementarity. Which substitution in Ivy would most plausibly reduce inhibitory potency by introducing steric clash without compensating interactions?

If blood is put into a collection tube without an anticoagul…

If blood is put into a collection tube without an anticoagulant, allowed to coagulate for 15 minutes, then centrifuged, the fluid part of the blood will be called ___________________. *One word answer. Use all lowercase letters. *Do not add any spaces or punctuation before or after the answer.

The excerpts below were obtained from a 2022 Journal of Biol…

The excerpts below were obtained from a 2022 Journal of Biological Chemistry publication called “Structural basis for the in vitro efficacy of nirmatrelvir against SARS-CoV-2 variants”. In Figure 2, nitrogen atoms are colored blue, sulfur atoms are colored yellow, and oxygen atoms are colored red. Nirmatrelvir is known to form a reversible covalent bond to Cys 145. What is the side chain of Cys that is involved in the formation of the covalent bond?