Benson Idahosa University
BCH 211: Biochemistry -General and medical 1
Practice 234+ past questions for BCH 211 (Biochemistry -General and medical 1) at Benson Idahosa University. Organized by topic with explanations. Free preview on Testwiz.
About BCH 211 at Benson Idahosa University
BCH 211 (Biochemistry: General and Medical 1) at Benson Idahosa University (BIU) introduces students to the fundamental principles of protein structure, function, and analysis. The course covers sequencing large polypeptides, protease cleavage specificity (e.g., trypsin), Edman degradation, SDS-PAGE, column chromatography, and protein fractionation methods. It also explores tertiary and quaternary structure, hydrophobic interactions, disulfide bond location, conjugated proteins and prosthetic groups, peptide bonds, and the biological roles of glucogenic amino acids. This course is designed for undergraduate students in biochemistry, medicine, and related life sciences who need a solid foundation in protein chemistry.
Practicing past questions by topic on Testwiz helps you master BCH 211 by reinforcing key concepts and techniques. Topic-based practice allows you to focus on challenging areas like predicting trypsin cleavage sites or interpreting chromatography results. Repeated exposure to exam-style questions improves recall, speed, and confidence, ensuring you are well-prepared for BIU assessments.
Topics covered
Sample questions
1. Which of the following BEST describes the role of proteases in sequencing a very large polypeptide?
2. Trypsin catalyzes the hydrolysis of peptide bonds in which the carboxyl group is contributed by which of the following amino acids?
3. A polypeptide contains six lysine and arginine residues. What is the expected number of smaller peptides produced upon complete cleavage with trypsin?
4. Which of the following statements about the hydrophobic side chains in tertiary structure is TRUE?
5. Which of the following amino acids is classified as a glucogenic amino acid?
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Get started freeFrequently asked questions
How do you predict trypsin cleavage sites in a polypeptide?
Trypsin cleaves peptide bonds specifically at the carboxyl side of lysine (K) and arginine (R) residues, unless the next residue is proline (P). To predict cleavage, identify each K or R in the sequence and cut after it, skipping any K/R followed by P.
What is the difference between Edman degradation and SDS-PAGE?
Edman degradation is a chemical method used to determine the N-terminal amino acid sequence of a polypeptide, removing one residue at a time. SDS-PAGE is a gel electrophoresis technique that separates proteins based on molecular weight, using SDS to denature proteins and impart a uniform negative charge.
Why are hydrophobic interactions important for tertiary protein structure?
Hydrophobic interactions drive the folding of proteins by burying nonpolar side chains in the interior, away from water. These interactions stabilize the tertiary structure by reducing the entropy of water molecules and are a major force in maintaining the protein's three-dimensional shape.
What are glucogenic amino acids and their biological role?
Glucogenic amino acids are amino acids that can be converted into glucose through gluconeogenesis. Their carbon skeletons are metabolized into intermediates like pyruvate, oxaloacetate, or α-ketoglutarate, which can be used to produce glucose, especially during fasting or low-carbohydrate conditions.