The final four questions will require you to determine whether the compound in question will partition into the organic or aqueous phase. Which layer will phenylalanine partition into? Note: look up "zwitterions"       water     diethyl ether

Knowing the functional groups of this molecule, which tests would possibly work to make positive and the color it forms, if it's negative leave blank with the benedicts yest,fermentation test, iodine test,seliwsnoffs test biurets test ninhydrin test, and xanthoproetic test which is positive with this structure

As we’ve discussed, a peptide bond is made when amino group of one amino acid combines with the carboxylic acid group of another amino acid (releasing a water molecule in the process). The C-N bond formed in this process is called a peptide bond. Peptide bonds have a few properties that might be unexpected. b) Another observation is that although the N-H of the peptide bond is able to serve as a H-bond donor the N atom of the peptide bond does not serve as an effective H-bond acceptor. Provide an explanation for this observation, using Lewis structures, VSEPR theory and/or valence bond theory as appropriate.c) It is also fairly accepted that while proteins undergo dynamic motions and conformational changes, and while R groups can freely rotate about Cα, it is generally not possible to freely rotate around a peptide bond. Please explain this observation, using a picture showing relevant orbitals on relevant atoms (your answer for part (a) might provide a useful basis for your reasoning…

Draw structures from notations or notations from structures, for the following tripeptides. (EOCQ 62) it. For drawing the structure of a tripeptide, follow the hints given in the previous question; you will have to connect three amino acid molecules in the specified order. а. Cys-Gly-Ala b. Ser-Leu-Val Нон НОН Но С. H,N-C-C-N-Ç-C-N-C-C-OH CH,CH,CHCH, CH3 C,H,CH, НОНН онНО d. H,N-C-C-N-C-C-N-Ç-C-OH CH,SCH,CH, CH-CНОН НSCH,

Q3: Use arrows to match the terms (A) column with (B) column. Some may be used more than once and others not at all. 1- Tirglyceride 2- Glycogen 3- Sphingomyelins 4- Membranes 5- Starch 6- Proteins 7- Cholesterol 8- Lactose B a- contain glycerol backbone b- glucose é- amino acids d- esters of fatty acids e- octapeptide f- disaccharide g- polysaccharide K- compound lipids i- steroid-like j- lipids k- polar lipids + glucose storage in animals 9- Waxes 10AngiotensinlI

Glycosaminoglycans (GAGs) are heteropolysaccharides composed of repeating disaccharide units. These units have some similar characteristics that allow them to be identified as GAGS. Which of the structures are examples of glycosaminoglycans? А. C. E. HO HO COO™ H Н ОН Н CH₂OH H H H OH OH Н CH₂OH Н OH H ОН o,so H H Н CH₂OH H H ОН H CH₂OSO H NH C=0 CH, H H Н NH c=0 CH3 H CH,OH OH Н ОН OH H B. D. Н НО H ОН H CH₂OH H ОН Н СОО ОН Н Н H H OSoz H Н OH б H CH₂OH ОН CH₂OSO H ОН H Н OSO, H Н NHSO,

Explain why casein is not denatured by the addition of acid (unlike most proteins).

A solution contains serine and alanine. What are the possible dipeptide products that can form from this mixture? H H H H N C -H N C O-H H CH₂OH H CH3 serine (ser) alanine (ala) Enter each answer as two three-letter codes joined with a dash (e.g. ala-ala).

Explain why casein precipitates when vinegar is added. Why was milk or raw egg once used as an antidote in cases of heavy metal poisoning? Based on your isolated yield of casein, how many grams of the protein are in one 200 g glass of milk? Which of the solutions contained amide bonds? Which test tells you this? Which of the solutions contained compounds with primary amino groups? Which test tells you this? Describe two examples of protein folding patterns and identify what level of protein structure they belong to. What other reagents might you use besides ferric chloride to test affinity for metal ions?

Which of the following is the primary driving force in the folding of a protein? a) The increase in entropy of the protein as it shifts to the final folded structure. b) The formation of stabilizing hydrogen bonds in the secondary structures. c) The formation of stabilizing disulfide bonds. d) The increase in entropy of the surrounding water as the protein folds e) The association of dipole/dipole interactions among charged amino acids