What is the thermodynamic driving force behind the formation of a peptide bond and how does it relate to the properties of the amino acid residues involved?
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- [Ten - Biomolecules] INSTRUCTIONS — Answer the following multiple-choice questions and EXPLAIN in 3-5 sentences why you chose that answer. — Answer properly Questions; Thomas was purifying an enzyme from a homogenate of muscle cells. He went through seven steps of purification and found that the enzyme activity was the same as the homogenate value. On the eighth step, when the protein washighly pure, the enzyme activity rose to five times that of the homogenate value. Can you suggest a possible reason? A. the homogenate assay was wrong B. step eight has co-purified an activator of the enzyme. C. the enzyme has an inhibitor present in the muscle cell homogenate D. the temperature at step eight was just right for the enzyme activity.Question: 1. Identify the amino acids in this peptide 2. Which amino acid sidechains are protonated at physiological pH 3. What is the overall charge of this peptide H₂N O NH₂ IZ ZI O OH IZ OH OHQUESTION 2 Which peptide will most strongly attach to a carboxymethyl ion exchange column at pH 7.4? O N'-Glu-Lys-Arg-Asp-Tyr-C' O N'-Tyr-Arg-Lys-Arg-Gly-C' O N'-Gly-Glu-Gln-Asp-Asp-C' O N'-Val-Ala-Leu-lle-Arg-C' QUESTION 3 Which will be product of transcription from this double-stranded (ds) DNA sequence? 5' - atgttcaaagcctattcg - 3' 3' - tacaagtttcggataagc - 5' O YKFRIS O uacaaguuucggauaagc O auauucaaaaccuauuca Which will be product of transcription from this double-stranded (ds) DNA sequence? 5' - atgttcaaagcctattcg – 3' 3' - tacaagtttcggataagc – 5' O YKFRIS O uacaaguuucggauaagc O auguucaaagccuauucg Ο MFKAYS QUESTION 4 The structure of hemoglobin consists of a 2a and 2B heterotetramer. O quaternary O tertiary O secondary O primary
- Question:- Alpha-endorphin is a peptide with an amino acid sequence of YGGFMTSEKSQTPLVT. How many charges does it have at pH 7?Denaturation of Proteins The following are four levels of protein structures. Identify the inter- and intramolecular forces of attractions that stabilized each level. Level of Protein Structure Forces of Attraction Present Primary Secondary Tertiary Quaternary 2.) What is denaturation? 3.) What are denaturing agents? Give three examples and describe their effects on protein. 4.) Differentiate reversible and irreversible denaturation. 5.)Why is 70% ethanol is more effective than 100% ethanol to kill bacteria?Question:- What is an example of a heterotrimeric G protein and what role does it play?
- Components of Complex Biomolecules Figure 1-10 (Lehninger's Biochemistry book) shows the major components of complex biomolecules. For each of the two important biomolecules below (shown in their ionized forms at physiological pH), identify the constituents. And show H-bonding with water. (a) Guanosine triphosphate (GTP), an energy-rich nucleotide that serves as a precursor to RNA: N- NH -CH2 0- NH2 H H H H. ОН ОН (b) Phosphatidylcholine, a component of many membranes: CH3 O- CH3*N-CH2-CH2-0-P-0–CH2 нн CH3 НС —О—С—(CH), —С—С— (CH), — СHз CH,–0-C-(CH,)14–CH3Need help The β chains of HbA and HbS were treated with trypsin, and the sequence of the N-terminal tryptic peptides are as given below. Do these peptides separate from each other in an electric field if the pH is 7.0? Explain in detail the reasoning behind your answer and include your calculations for the charge of each peptide in your answer. HbA: Val-His-Leu-Thr-Pro-Glu-Glu-Lys HbS: Val-His-Leu-ThrpH 6.2 Aspartate Glycine Histidine unknown Leucine Proline Lysine By looking at the electrophoretogram, and providing the answers in the box below, indicate: ) which of the known (!) amino acids are potentially at/ near their isoelectric point. Justify your answer by describing their relative migration compared to the origin and deduce their overall charge. i) Using one of these amino acids, describe how it meets the definition of being isoelectric by describing the protonation/ deprotonation state of all of the ionisable groups, and hence its overall charge. "
- Question 11. // Hint: Isoelectric focusing separates proteins based on their pI values, and can separate proteins that only differ by a net charge of ±1.±1. Recall that an amino acid residue with a negatively charged R group has a relatively low isoelectric point (pI) where it has zero net charge. Likewise, an amino acid residue with a positively charged R group has a relatively high isoelectric point (pI) where it has zero net charge. Order from Low pH to High pHQuestion:- Give a brief description of what the term ‘native protein’ state refers to. Your answer should make a specific reference to how the structural organisation of this state is accomplishedSaved Question 264 At pH 12.48, arginine (pK's 1.82, 8.99, 12.48) would be charged as follows: O 1) -1 alpha-carboxyl, 0 alpha-amino, +0.5 guanidino, -0.5 net charge O 2) 0 alpha-carboxyl, 0 alpha-amino, +1 guanidino, +1 net charge 3) +1 alpha-carboxyl, -1 alpha-amino, -1 guanidino, -1 net charge O4) +1 alpha-carboxyl, 0 alpha-amino, -1 guanidino, O net charge 5) 1 alpha-carboxylate, +1 alpha-amino, +1 guanidino, +1 net charge