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- Metalloprotein linkages are most likely to be formed between: a.Two cysteines b.An arginine and a glutamic acid c.A leucine and a phenylalanine d. Two aspartate residues e.A tyrosine and a serine3b) Both a-helical 2° structure and b-pleated sheet 2° structure result from the same type of interaction; briefly explain in your own words why you might observe an a-helix in one region of a protein and a b-pleated sheet in another region of the same protein.6.Provide the structures and functions of three biochemically important disaccharides
- 1.a.If this molecule was the side chain of an amino acid, in a protein, what tertiary structure stabilizers could be present? b.Make a key and use color to highlight what part of you structure can be stabilized in each manner?What is the primary reason the a-helix conformation in polypeptides such a stable form? A. The a-helix structure is stabilized by hydrophobic interactions. B. The a-helix structure is stabilized by intra-helical hydrogen bonds. C. The a-helix structure is stabilized by disulfide bonds. D. The a-helix structure is stabilized by proline residues.46. The SH2 protein domain has 2 binding sites: one for ________ and one for _________. A. Phosphotyrosine; {a}- methyltyrosine B. C- Terminus; N-terminus C. Phosphotyrosine; flanking amino acids D. Alpha Helices; Beta-Pleated Sheets
- 4. Amino acids are linked together by peptide bonds to form polypeptides. (a) Draw the structure of a tripeptide (b) draw an asterisks (*) directly beside all alpha carbons and draw a square around all peptide bonds (c) Use arrows to identify and label the N-terminus and C-terminus (d) Draw a circle around the R group of each amino acid residue in the tripeptide and classify each R group as polar, non polar, acidic, or basic (e) Using the abbreviated names of the amino acids, provide the primary structure of the tripeptide you have drawn.What protecting groups in solid-phase peptide synthesis NOT do? a)Activate the carboxlic acid to have a good leaving group b)Prevent the amino acid backbones from randomly polymerizing in solution c)Prevent the amino acid side chains from undergoing uncontrolled chemistry d)Get cleaved from the peptide when the peptide is cleaved from the resin7/ Hemoglobin is an example of a protein with A. Primary structure only. B. two protein chains held together. C. a quaternary structure. D. primarily a B-pleated sheet structure.
- Explain what is meant by “The Central Dogma”? In your explanation, describe the structure and function of the macromolecules that are important in this process. Describe at least 4 deviations to the Central Dogma.1. (a) Draw a circle around one amino acid in the structure. (b) Draw a box around one amino acid side chain. (c) Indicate whether the side chain you chose is hydrophobic or hydrophilic. (d) Draw an arrow pointing to a peptide bond 2. If the peptide segment shown above was part of a beta sheet, which of its functional groups would be involved in forming and stabilizing the beta sheet? 3. Which amino acid (also called amino acid residue)would be more likely to occur on the surface of a protein: an aspartate residue or a methionine residue? Explain your choice.59. Which of the following statements is FALSE? Select one: a. G-C bonds are much more resistant to denaturation than A-T rich regions. b. The sugar contained in RNA is a ribose. c. Thymine is present in RNA. d. The two strands of DNA run antiparallel to each other.