Based on their fat content, which is the healthier option? Explain your answer. - Based on all of the nutritional information, which do you think is the healthier option? Explain your answer.
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Using the image provided, answer the two questions:
- Based on their fat content, which is the healthier option? Explain your answer.
- Based on all of the nutritional information, which do you think is the healthier option? Explain your answer.
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- please help me understand asap Please draw by hand a tripeptide of Glu, Gln, and 1 amino acid of your choice (Not Glu or Gln again) at pH 7.0 and 9.0. The only requirement is that the amino acid should be 1 of the amino acids with ionizable R groups. Peptide should have appropriate charges on groups. Please. Provide an explanation for the fact that a-D-mannose is more stable than B-D-mannose, whereas the opposite is true for glucose.IX. Insulin, a hormone vital in blood sugar regulation and having a polypeptide chain with disulfide linkages, loses its regulatory activity when heated at nearly 100°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of insulin relative to its native structure and function. I--
- Peptides. 1. Draw the peptide Ala-Glu-Gly-Lys, as it would occur at physiological pH = 7.4. The R groups of Ala and Gly are not acidic or basic, therefore do not have a pka and the charge on these R groups is therefore independent of pH. Glu is acidic and Lys is basic, therefore the charge on these amino acids is pH dependent. The pKas are shown below. pKa N-term = 9.0 C-term = 3.5 Glu4.1 Lys = 10.5 2. Draw a circle around the peptide bonds. 3. Label the C-terminus and the N-terminus. 4. What is the overall charge on the peptide at pH 7.4?Protein,nfolded Proteinţolded Under certain conditions, a specific protein has the following thermodynamic parameters for going from the unfolded state to the folded state: AH = – 300 kJ/mol, and TAS = – 400 kJ/mol. Under those conditions, the equilibrium would lie more toward neither would predominate - the fraction of total protein that's folded would = fraction unfolded. the folded state the unfolded state O It is impossible to predict the position of the equilibrium from AH and TAS.Malonyl-ACP is a precursor in fatty acid synthesis in the acyl carrier protein pathway. Draw the structure of malonyl-ACP No stereochemistry required Represent ACP by R1 and be sure to include charges on atoms at ph=7
- Drawing the Structure of a Glycopeptide (Integrates with Chapters 4and 5.) Consider the peptide DGNILSR, where N has a covalentlylinked galactose and S has a covalently linked glucose. Draw thestructure of this glycopeptide, and also draw titration curves for theglycopeptide and for the free peptide that would result from hydrolysis of the two sugar residues.Hi - I have the following as a question in my biochemistry course and I am just lost on where to start. Thanks! Cyt cb562 will form a tetramer in the presence of Zn+2 or in the absence of Zn+2, it will form a trimer. For both the tetramer and the trimer, suggest the identity of three different amino acids that could be on the interface. Explain how your selections facilitate these interactions.R V. Phospholipids are the main structural lipids that comprise cellular and organellar membranes. One abundant phospholipid in bacterial cell membranes is phosphatidylethanolamine (PE), which has a generic structure shown on the right. Note that R1 R and R2 are representative alkyl chains of attached fatty acids, each having about 16 – 20 carbon atoms. a) The overall net charge in one PE molecule is: -2 -1 0 +1 +2 CH₂ Phosphatidylethanolamine (PE) -CH H₂C. b) The glycerophosphate backbone in PE is a: D-enantiomer c) The fatty acids are attached to PE via which type of bond? amine L-enantiomer racemic NH3 amide ester ether d) Draw the commonly used cartoon representation of one phospholipid molecule. Label the hydrophilic and hydrophobic parts.
- Need 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-Thr1,2-dioleoyl-3-myristyl-sn-glycerolsn-16:0-12:0-16:0LLnO Consider the TAGS abovea. Which is most prone to lipid oxidation? Explain.b. Which has the highest melting point? Explain.c. Which will most likely convert fastest to the most stable polymorphic form. Explain.. Separating Glycated Hb From Normal Hb (Integrates with Chapters 5and 6.) Human hemoglobin can react with sugars in the blood(usually glucose) to form covalent adducts. The a-amino groups ofN-terminal valine in the Hb b-subunits react with the C-1 (aldehyde)carbons of monosaccharides to form aldimine adducts, whichrearrange to form very stable ketoamine products. Quantitation ofthis “glycated hemoglobin” is important clinically, especially fordiabetic individuals. Suggest at least three methods by which glycatedHb (also referred to as HbA1c) could be separated from normal Hband quantitated