3. Given the following peptide sequence, GSICDNCR, the estimated net charge at the given pH is: a) -2 at pH 13.5 b) -1 at pH-11.5 c) +1 at pH-6.5 d) +2 at pH-5.5 e) 0 at pH-4.5
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Solved in 3 steps
- 1. The chromatography solvent is very polar as it contains alcohol, an acid and water. Based on this information, list all the polar amino acids and arrange them from most polar to least polar.4. What is the region/point where AA is predominantly present as a (-2)-charged species?5. The effective buffering range for the amino acid in the acidic region is?6. What is the region/point where the solution has a 50:50 percent mixture of the (0) and the (-1) species?1. Describe how each of the following relates to protein configuration: primary structure - secondary structure - tertiary structure - quaternary structure -
- 1)Explain 3 benefits of proteins forming higher oligomeric states. 2) Why are peptide bonds planar?4. Amino acids are linked together by peptide bonds to form polypeptides. (a) Draw the structure of a tripeptide (b) draw an asterisks (*) directly beside all alpha carbons and draw a square around all peptide bonds (c) Use arrows to identify and label the N-terminus and C-terminus (d) Draw a circle around the R group of each amino acid residue in the tripeptide and classify each R group as polar, non polar, acidic, or basic (e) Using the abbreviated names of the amino acids, provide the primary structure of the tripeptide you have drawn.1.What reactive groups are involved in the formation of a peptide bond?2.A molecule of what substance must be removed in order to form a peptide bond?
- 1. Which peptide would be more soluble at pH 7.0, (Val)₂₀ or (Asp)₂₀ ? at pH 3.0, (Gly-Glu-Val)Your vaccine will be administered as a topical cream, and you require your peptide to have an overall neutral charge in order to be functional. At what pH should you formulate your cream to maintain a neutral charge on the peptide? Why is this a good pH?6.All of the following types of interactions cooperate in stabilizing the tertiary structures of globular proteins except____. a.Disulphide bond b.Hydrogen bond c.Ionic interactions d.Peptide bond
- What is the monomer of a nucleic acid macromolecule?Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary and secondary (b) primary and tertiary (c) secondary, tertiary, and quaternary (d) primary, secondary, and tertiary (e) primary, secondary, tertiary, and quaternaryThe first and major effect in denaturation of proteins is that: a. peptide bonds break. b. helices unwind. c. sheet structures unfold. d. tertiary structure is changed. e. quaternary structures disassemble.