Medical Biochemistry Unit 1 Week 1 Assessment with Verified Answers| 100% Correct| 100% Score

Which of the following best describes tertiary structure? - Interactions between α-helices and β sheets to form a domain. Tertiary structure is best described as the entire three-dimensional conformation of a polypeptide including how secondary structural features - helices, sheets, bends, turns and loops - assemble to form domains and how these domains relate. Which of the following best describes the structure of heme? - A planar porphyrin ring that binds iron Heme is a prosthetic group that is planar and has a bound iron center. Covalent catalysis is used by many enzymes to cleave peptide bonds. Which of the following amino acids would not facilitate this type of catalysis? (Think of the structure of the R-group of these amino acids) - Valine The R-group on valine does not have an active group to participate in covalent catalysis. The most commonly participating amino acids are cysteine, serine and histidine. An enzyme has a mutation within the substrate binding site that reduces the binding of the coenzyme needed for covalent catalysis. Which of the following is likely to result as a consequence of this mutation? - The enzyme will not be able to form the transition state complex Loss of coenzyme binding will result in inability to form the transition substrate enzyme complex. Movement of ammonia from an amino acid to an α-keto acid involves a family of enzymes best categorized as which of the following? - Transferases