Lysine (polar basic) > serine(polar , neutral) > phenyl alanine (non polar , neutral)
C. AMINO ACIDS AND POLARITY Suppose you had a mixture of the following amino acids in...
b. A person eats mushrooms because he hears that they contain "enzymes that are good for you."What is the end product of digesting mushroom proteins? Do you think the enzymes” would be active after digestion? B. DIPEPTIDES Draw the two dipeptides which can be formed from serine and cysteine. Circle the amide bonds. Hint: It helps to draw the amino group to the left and carboxyl to the right when orienting the amino acids. Ser-Cys Cys-Ser C. AMINO ACIDS AND...
Q.2. How to separate the mixture of the following amino acids (alanine pl = 6.01); lysine (pl = 9.74) and aspartic acid (pl = 2.77) with the use of gel electrophoresis and the buffer of proper pH. Suggest buffer pH and present the order of investigated solute migrations. Buffer pH = Order of solute migrations toward cathode.
Fill in the blanks for each amino acid
Amino Acid Properties Name of R-group Properties Amino Acid Type of Polarity pKa Charge at Special functional group pH-7 Properties (hn(wpp)amgies applicable) (whpee Alanine Arginine Asparagine Aspartate Carboxyl Polar 3.9 Sulfhydryl Polar N/A Forms S-S Glutamine Glutamate Histidine Isoleucine Lysine Methionine Phenylalanine Aromatic Non-Polar Absorbs G@ 280 nm N/A Proline Can be Serine Threonine Tryptophane Tyrosine Valine
Which of the following amino acids will be retained longest in the column when separated by cation-exchange chromatography? H 1. Serine HO-CH2-C-COO® IV. Lysine NH H3N-CH2CH2CH2CH2CH -COOH NH H H V. Phenylalanine -CH--COOH NH II. Alatine Chy-d-coop H II. Cysteine HS-CH -¢-Coo® NH О О О О О IV V
#202 Dipeptides Which amino acids, in order left to right, are present in the following structure? HN OH Select one: O a. tyrosine, serine O b. tyrosine, threonine c. phenylalanine, threonine d. phenylalanine, valine e. phenylalanine, isoleucine O
9) What type of attraction would you expect between the R groups of each of the following amino acids in a tertiary structure of a protein? (see Table 16.2) a) proline and phenylalanine b) Aspartate and arginine c) Tyrosine and water d) Cysteine and cysteine e) Serine and tyrosine f) Leucine and alanine 2
9) What type of attraction would you expect between the R groups of each of the following amino acids in a tertiary structure of a protein?...
) You have a mixture of serine, aspartic acid, and histidine. A) Find a pH value that would separateApply the sample here. the three amino acids from each other B) Draw the structure of serine, aspartic acid, and histidine at the pH chosen in part A. C) Draw how they would move in an electric field at the pH you have chosern. Apply the sample mixture here
Which of the following amino acids may alter the direction of a polypeptide chain and cause a section of this chain to bend? a. phenylalanine b. serine c. proline d. histidine e. tryptophan
For the following questions, consider six proteins, each 50
amino acids long, made of just a single type of amino acid. Protein
P is made of proline; K, lysine; S, serine; E. glutamic acid; F,
phenylalanine.; and G. glycine. Your answers are going to be P, K,
S, E, F or G.
1. Which of these proteins would move fastest on SDS-PAGE?
2. Which of these proteins would move fastest on Sephadex?
3. Which of these proteins would move closest...
Question 10 (10 pts) Peptides are biological oligomers formed by condensing multiple amino acids into an amide backbone. Although this amide backbone is common to all peptides, the so- called 'side-chan' groups attached to this backbone vary depending the amino acids used in the condensation reaction. Shown below are four different tetrapeptides (so-named because they are the products of the condensation of four amino acids). Based on their structures, predict the order of elution that one might expect if separating...