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- 1. Type of bond a. H-bond b. Electrostatic interaction c. Hydrophobic bond d. Disulfide bond e. Peptide bond 2. Level of protein structure a. primary b. secondary c. tertiary d. quaternary 3. Method/s of denaturation. choose all that applies a. Heating to 100 degrees Celsius b. Addition of nitric acid c. Reaching Isoelectric point d. Addition of mercuric chloride e. Addition of sulphosalicylic acid f. Addition of alcohol g. Addition of ammonium sulfate43. Specify expressions specific to panaxosides. I. taken from ginseng II. there are glucose and arabinose monosaccharides in this compound III. taken from Japanese angelica-tree IV. tetratcyclic triterpen saponins V. spirostanol type glycoside VI. dimer structure VII. biglycosides VIII. dammaran group IX. differ for number of hydroxyl groups X. furostanol type glycoside A) II; VI; VII; IX; X B) III; V; VIII C) I; IV; VIII; IX D) I; VIII; IX E) I; III; V; VII; VIII; X16. Describe the basic principles behind the functioning of an amino acid analyzer. What is it? W- is it used for? How does it work (start to finish)? 17. In peptide, protein chemistry, what does the term 'sequence' mean? 18. About how many amino acid residues can be in a peptide in order to sequence it by Edman degradation?
- your name, and ID on your scantron. 1. The following Haworth projection for sure is? a. d 2. The compound is question 1 is? a alpha a. danose b/D 3. The compound in question 1 is a? furanose a. b. beta fructose HO b. galactose c./ 4. The compound is question 1 is a closed form of? OH c. gamma OH c. pyranose cglucose FOH OH d. L d. epsilon d. thanose d. sucrose e. not a.-d. e. not a.-d. e. not a.-d. e. not a.-d. try a. -C tDescribe what each reagent does in SDS Page 1. Sodiun dodecyl sulfate 2. Polyacrylamide 3. MercaptoethanolAn amino acid that has an indole group side chain.a. Trpb. Phec. Tyrd. Pro
- 1. The Ability of a substance to exist in different crystalline form a. Lattice b. Polymorphism c. Crystallization d. Amphoterism 2. A drug can exert its pharmacological effect only if it is a. Protein bound b. Protein unbound c. Free drug d. Both B & C e. Both A & C 3. In order for the drug to be ready and available for absorption, it must be release first from its dosage form with the exception of: a. Capsule b. Tablet c. Solution d. Suspension 4. All of the following are true, except a. Solubility increase with decrease particle size b. Solubility increase with increase surface area c. Solubility increase with increase particle size d. Solubility decrease with decrease surface area 5. The rate in which the drug appears in the bloodstream is also known as a. Half-life b. Potency c. Bioavailability d. Area under the curveneed some help with this question can you help with the first partE (+)-cyanthiwigin-AC F MeMgCl H₂C*** g H₂C CH3 CH3 G PhSSO₂Ph 1. a. IBX b. MMP c. K₂CO3 H₂C H Į HCI SPh CH3
- 2. Diagram the peptide ACKE at physiological then answer questions a- h. a. Circle one peptide bond. b. Box one alpha carbon in this peptide c. How many peptide bonds are present in this peptide? d. Which amino acid is at the C-terminus? e. Which amino acid is at the N-terminus? f. Label one omega, one phi and one psi bond angle. g. Sketch in one peptide plane. h. Calculate the charge of the peptide at pH 13.A1c Select ONE peptide linkage and draw a circle around all of the atoms that would lie in a single plane. H R2 | H H;Ñ. || C. N R, H H R3 H Ilt. O=0Disulfide linkages: A. are covalent bonds. B. are a type of electrostatic interaction. C. occur between methionine residues. D. can be disrupted by SDS. E. can only occur within the same polypeptide chain.