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Biochem ACS Study Guide Questions and Answers

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Which Amino Acids will be charged at pH 7? Ans- DEHRK: Aspartic Acid (Asp), Glutamic Acid (Glu), Histidine (His), Arginine (Arg), Lysine (Lys) Which amino acids will have a negative charge at pH 7? Ans- D&E: Aspartic Acid (Asp) and Glutamic acid (Glu) Which amino acids will have a positive charge at pH 7? Ans- H, R, K: Histidine (His), Arginine (Arg), Lysine (Lys) Which of the following sequences are most likely to be in the interior core of a globular protein? (A) ITFWLI (B) IKFGVA (C) DKYPGE (D) MPCDNA Ans- The interior is hydrophilic so sequence: ITFWLI is most likely to be in the interior because there is no charged amino acids and had the lowest percentage of polar amino acids. How are beta sheets stabilized in proteins? Ans- Hydrogen bonding between peptide backbone groups. Fibrous Proteins Ans- Not water soluble, not flexible in secondary structure, highly repetitive primary structure, elongated structure; 2 α keratin polypeptides each which forms an α helix twisting around each other to form a left handed coil. Globular Proteins Ans- Water soluble, flexible in secondary structure, not necessarily highly repetitive, size and ability to associate into a larger structure varies. Gel filtration elution Ans- Largest elutes firs

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Biochem ACS Study Guide Questions and Answers Which Amino Acids will be charged at pH 7? Ans- DEHRK: Aspartic Acid (Asp), Glutamic Acid (Glu), Histidine (His), Arginine (Arg), Lysine (Lys) Which amino acids will have a negative charge at pH 7? Ans- D&E: Aspartic Acid (Asp) and Glutamic acid (Glu) Which amino acids will have a positive charge at pH 7? Ans- H, R, K: Histidine (His), Arginine (Arg), Lysine (Lys) Which of the following sequences are most likely to be in the interior core of a globular protein? (A) ITFWLI (B) IKFGVA (C) DKYPGE (D) MPCDNA Ans- The interior is hydrophilic so sequ ence: ITFWLI is most likely to be in the interior because there is no charged amino acids and had the lowest percentage of polar amino acids. How are beta sheets stabilized in proteins? Ans- Hydrogen bonding between peptide backbone groups. Fibrous Pro teins Ans- Not water soluble, not flexible in secondary structure, highly repetitive primary structure, elongated structure; 2 α keratin polypeptides each which forms an α helix twisting around each other to form a left handed coil. Globular Proteins Ans- Water soluble, flexible in secondary structure, not necessarily highly repetitive, size and ability to associate into a larger structure varies. Gel filtration elution

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