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. If a key Ivy residue that donates a hydrogen bond to a catalytic residue in lysozyme is mutated from Ser to Val, which outcome is most likely?
Read DetailsThe information below are excerpts from a 2025 publication i…
The information below are excerpts from a 2025 publication in Nature titled “Structural and functional characterization of human sweet taste receptor”. The researchers report in the paper that several mutations in the T1R2 Venus flytrap (VFT) domain alter responses to natural sugars. Which outcome best supports a direct ligand-contact role for a given residue?
Read DetailsThe 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. In addition to a covalent bond with the active site Cys sidechain, Glu 166 also participates in inhibitor binding. Which of the following correctly describe the nature of the interactions between the inhibitor and Glu 166?
Read DetailsPlease upload the scan of your exam here. Remember that it…
Please upload the scan of your exam here. Remember that it needs to be a SINGLE pdf file in portrait orientation with clear, legible work in numerical order and final answers clearly marked. Questions with multiple parts (a, b, c, etc.) need to be labeled. This link will take you to your K-State email, if needed. outlook.office365.com
Read DetailsThe figure below is an excerpt taken from a paper titled “Ch…
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. 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 graphs presented in Figure 1 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). Finish the following sentence: “Based upon the plots, the fatty acids bind ____ to the recombinant mutant HSA than they bind to the wildtype HSA”
Read DetailsAssume that the consumption function is given by C = 200 + 0…
Assume that the consumption function is given by C = 200 + 0.7 (Y − T), the tax function is given by T = 100 + t1Y, and Y = 50K0.5L0.5, where K = 100 and L = 100. If t1 increases from 0.2 to 0.25, then consumption decreases by:
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