Which amino acid doesn't show optical activity? Why?
GLYCINE
it is the simplest amino acid it doesn't have the
Stereoisomer.
It is the only amino acid that is optically active.
This amino acid is essential for biosynthesis for
Nucleic acid as well as bile acid
SHOW WORK 1. Why is an amino acid called an amino acid? Use the following structure for questions 3-6. The circle contains the side chain of the amino acid Lysine (Lys). I 2 Is the side chain polar or nonpolar? 3. Is the side chain hydrophilic or hydrophobic? 4. Is the side chain acidic; basic, or neutral? 5. What is the name of the functional group in the side chain? 6 What is the strongest attractive force for the side...
Val-Tyr is a dipeptide consisting of valine and tyrosine amino
acid that exhibits antihypertensive activity. Show the mechanism
(including electron pushing arrows) for the phophorylation of
Val-Tyr by ATP. Remember, you can use R groups to simplify complex
molecules.
ОН R1 NH3 АТР Val-Tyr
For the following amino acids - explain why the overall charge on the amino acid is different at PH's 2, 7, and 11. Relate it to the pk, of the groups on the molecules To achieve distinction, you must explain that the form of an amino acid, whether positively charged, negatively charged or neutral, depends on the pH of the solution and also on the Ka of the acid group
which part of amino acid is always acidic?
Which part of an amino acid is always acidic? Amino functional group Side chain ("R group") None of the above Carboxyl functional group
Which of the following amino acid side chains would be classified as a polar neutral amino acid? Which of the following names identifies an enzyme? substrate glycolysis phosphoglucose dehydrogenase A protease cleaves what bond in its substrate? phosphodiester hydrogen double peptide Monitoring protease activity in milk can be accomplished by using a spectrophotometer measuring what variable? diameter of clearing absorbance of light time concentration of milk
a) which amino acid tested is most polar?
b) look up the structure of the amino acids. explain why it
makes sense that the amino acid you listed is more polar than the
others?
c) what amino acids are in the fruit juice?
D. CHROMATOGRAPHY Chromatography is a general technique that is used to separate various materials. In this case, students can use the unique chemistry of the amino acid to determine its migration in a specific solvent. The solutions...
2. Amino Acids a.) Which amino acid is this: A substitution on the methyl group of this amino acid with a hydroxyl group yields the amino acid Ser and substitution with a phenyl group yields the amino acid Phe. b.) Which amino acid has an a-amino group that is bonded directly to two C atoms, forming a ring?
6. Why is it necessary to wear latex gloves when handling the amino acid chromatogram? 7. An amino acid travels 2.5 cm from the origin on a paper chromatogram, and the solvent front travels 7.5 cm. Show the calculation for the Rf value of the amino acid? 8. Why should a pencil – not a pen --- be used to mark the origin on a paper chromatogram? 9. What precautions should be observed in this experiment?
There are amino acid residue at the following positions: Arginine - 136 Valine - 58 Glycine - 235 Glutamate - 97 Which of the following amino acid substitutions would be least likely to affect the activity of this enzyme? Why? A. Tryptophan at position 235 B. Aspartate at position 58 C. Lysine at position 136 D. Asparagine at position 97
Which amino acid has a net charge of “+ 0.09” at pH 7? Show all calculations. Draw the structure of the amino acid that would predominate at this pH. (The answer should be Histindine; draw the structure of histidine. Calculate the net charge using a H-H equation. Please walk through every single step as if I was five years old I am very confused).