Q1: Please name the following amino acids( three letter name, for example: Ala for alanine) Q2: Which of them are hydrophobic aa, and which are hydrophilic COO COO H-C-CH2-SH H-C- CH2-CH2-CH -CH2-NH N Nht COO COO COO H-C-CH2-OH H-C-CH3 H-C—CH2 NH NH3 NH COO H CO0 C COO H—C-H CH H--C-CH2-CH2-C NH H N 1CH NI H
Q1: Please name the following amino acids (three letter name, for example: Ala for alanine). Q2: Which of them are hydrophobic AA, and which are hydrophilic?
Q3: Write down the dipeptide that can be formed with these two aa and indicate(1)the N-terminus and C-terminus,(2)which atom of the dipeptide can form hydrogen bond with any other dipeptide H R H N-CH-C-OH+ H-N-CH-CoO Q4 :(1) Do amino acids in a-helix or B-sheet form hydrogen bonds among the same polypeptide chain?(2)Do side chains of the amino acids contribute to the formation of the hydrogen bonds?
Q3: Write down the dipeptide that can be formed with these two AA, and indicate (1) the N-terminus and C-terminus, (2) which atom of the dipeptide can form hydrogen bond with any other dipeptide. Q4: (1) Do amino acids in a-helix or b-sheet form hydrogen bonds among the same polypeptide chain? (2) Do side chains of the amino acids contribute to the formation of the hydrogen bonds?
Q5: please indicate the a-helix, B-sheet and connecting loop in this figure representing the tertiary structure of a protein N B A C Q6: please list at least three important biological functions of proteins in cell
Q5: please indicate the a-helix, b-sheet and connecting loop in this figure representing the tertiary structure of a protein A B C Q6: please list at least three important biological functions of proteins in cell
Q7: Which of the following techniques are for protein purification, Which for primary structure determination, which for 3-D structure determination? What principal properties of the proteins are used for those techniques of protein purification? 1. Gel filtration chromotography X-ray crystallography 3. Edman degradation 4. Electrophorsis 5. NMR
Q7: Which of the following techniques are for protein purification, Which for primary structure determination, which for 3-D structure determination? What principal properties of the proteins are used for those techniques of protein purification? 1. Gel filtration chromotography 2. X-ray crystallography 3. Edman degradation 4. Electrophorysis 5. NMR