LLNSAMSRLYSLRSS 1.Assuming this sequnce is enitrely alpha helical what is the hydrogen bond donor to the carbonyl oxygen of Met6? 2.what amino acids in the sequnce above would most likely face the hydrophoic core od a protein? 3. at ph7 which amino acid side chain can form ionic bonds.
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LLNSAMSRLYSLRSS
1.Assuming this sequnce is enitrely alpha helical what is the hydrogen bond donor to the carbonyl oxygen of Met6?
2.what amino acids in the sequnce above would most likely face the hydrophoic core od a protein?
3. at ph7 which amino acid side chain can form ionic bonds.
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- 1. In a protein, why does when Ala is replaced with Ile, it loses its activity but when Lys is replaced by Arg and Leu to Ile, it only has little effect on protein structure and function? Explain. 2. Why do proteins cannot be denatured reversibly when they are chemically altered to change the chemical composition of certain side chains? Explain.Upload a drawing of Gly-Met-Asn-Glu-His Label the alpha carbons Label the R groups as hydrophobic or hydrophilic Label the acidic and basic R-groups Label the peptide bonds Label the N terminus and the C terminusAla-Arg-Val-His-Asp-Gln Given the polypeptide chain above Estimate the net charge of the polypeptide chain at physiological pH (7.4) and at pH 5.0 . How many peptide bonds are there? What kind of polypeptide is it?
- Topic: ISOLATION AND CHARACTERIZATION OF PROTEINS 1. Which amino acids contains the following:a. Sulfur/sulfhydryl groupb. Aromatic groupc. Imidazole ringd. Guanidine groupe. Indole ring2. Classify the following proteins to their biological functions (casein, albumin, gluten, andmyoglobin) 3. Which level of protein structure organization are lost hydrolysis and denaturation?4. What is the Beer-Lambert’s Law? Why is it relevant to the quantitative analysis of proteins?1. What is the isoelectric point (pI) of lysine which has pKa values of 2.1 for the α carboxyl group, 9.7 for the α amino group and 10.5 for the side chain amino group? 2. Which of the following is most likely to be found on the exterior of a protein? A) Pro B) Trp C) Ser D) Glu 3. The type of reaction that forms a peptide bond is A) Elimination B) Hydrolysis C) Nucleophilic substitution D) CondensationColor Reactions of Intact Protein: 1ml of water and 0.5 g of casein 1ml of water and 0.5 g of bean protein 1ml of water and 0.5 g of gluten
- A new amino acid is found with the alpha N and backbone COOH pKa's the same as histidine but with a neutral side chain. What is the isoelectric point of this new amino acid?Which intermolecular forces are important in acetic acid, CH3 –(C=0)-oh? A particular amino acid contains a- CHNH3+ group. Is this amino acid more likely to be found on the inside or the outside of the folded protein? Briefly explain. The addition of ethanol, CH3CHOH, t an aqueous solution lowers the surface tension of the solution. Predict whether adding ethanol to an aqueous protein solution will tend to stabilize or unfold the protein. Briefly explain.A. Consider the dipeptideVal–Pro: What amino acid is the N terminal aminoacid? What amino acid is the C terminal aminoacid? How are the amino acids connected? Give the name of the dipeptide. Give the name of the dipeptide in which the amino acid order is reversed as Pro–Val.
- 6. Which class or reactions results in the degradation of all macromolecules: a) dehydration synthesis of monomersà polymers with the loss of an H2O with the addition of each monomer b) hydrolysis with the addition of one H2O for each reaction c) oxidation with the loss of an e- d) reduction with the gain of an e-In α-helices - what is the length of the hydrogen bonds between: TYR41H and GLU37O ALA39H and MET35O GLU38H and ILE34O THR36H and ARG32O. ARG32H and TYR28Odoes all 20 amino acids soluble in organic solvents like acetone and chloroform? true or false
