1. Recognize the following types of biomolecules when given images such as the ones below and on the next page: • glucose (which is a monosaccharide) . polysaccharide ● amino acid ● ● ● protein (recall a protein with less than 50 amino acids can also be called a peptide whereas a protein with 50 or more amino acids can also called a polypeptide) steroids triglycerides phospholipids DNA ● RNA

1. Recognize the following types of biomolecules when given images such as the ones below and on the next page: • glucose (which is a monosaccharide) . polysaccharide ● amino acid ● ● ● protein (recall a protein with less than 50 amino acids can also be called a peptide whereas a protein with 50 or more amino acids can also called a polypeptide) steroids triglycerides phospholipids DNA ● RNA

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter3: The Chemistry Of Life: Organic Compounds

Section3.1: Carbon Atoms And Organic Molecules

Problem 3C

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a. what general category would you place this molecule in of the four categories of biomolecules? b. List 5 functional groups you see in this molecule?
8. Multiple choice. Which of the following is not a method that can be used to determine the 3° structure of proteins? (2 pts) a) Protein X-ray crystallography b)) Circular dichroism c) Cryogenic electron microscopy d) Protein NMR 9. Multiple choice. Approximately what overall yield can you expect from the solid phase peptide synthesis (SPPS) of a "10-mer" (a 10 amino acid peptide), if the yield from each step is 85%? (2 pts) 23% b) 20% c) 85% d) 71% 10. Multiple choice. Which protein purification method is best for an experiment in which you want to purify a monomeric form of a protein away from a tetrameric form? (2 ptrs) (-His a) Affinity chromatography S b) High pressure liquid chromatography c) lon exchange chrommatography d) Size exclusion chromatography 2. I1. Short answer. What is the Edman degradation experiment useful for? (3 pts) purdinate an for prry structers steps .
Given a peptide chain that is composed of the following amino acids:(branched chain-- polar uncharged--polar positively charged -- polar negatively charged-- aromatic) 10If the component amino acids of the above peptide chain are subjected to paper chromatography, which of the amino acids will be farthest from the point of origin?
H8. Protein A interacts with biomolecule B and forms a complex AB, with a dissociation constant KD = 1 µM at 25 °C, (for dissociation, AB ⇋ A + B, KD=[A][B]/[AB]). The interface contains a phenylalanine residue. A biochemist mutated the phenylalanine of protein A to a tyrosine (A’), which introduced a hydrogen bond between the hydroxyl group of the tyrosine with B without affecting any other interactions. The formation of the hydrogen bond releases a heat at 11.4 kJ/mol. What is the KD of the complex of the mutant A’ with B? Hint: Gas constant R = 8.3145 J/K/mol, Euler’s number e = 2.7183, ln(A) - ln(B) = ln(A/B).
Shown below is the structure of a polypeptide with the pK, values of its acidic hydrogens. pK = = 10.1 H OH pK, = 9.2 H. pKa = 2.1 H. N-H pK, = 6.0 pKa = 3.9 1. How many peptide bonds are present in one molecule of the polypeptide? [ Select ] II. Over what pH range would this molecule predominantly exist in a state that has a net charge of zero? [ Select ] ZI
Use any three amino acids from the picture below to form a tripeptide on paper and then upload the file here? Is this tripeptide soluble in water, why or why not? H. H3N+- CH2 H3N+ H3N+-C- H3N+. H3N+ H3C-CH CH2 CH CH3 CH H3C CH3 H3C CH3 CH3 Glycine (G) Gly Alanine (A) Ala Valine (V) Val Leucine (L) Leu Isoleucine (I) lle Nonpolar side chains H. H. H. H. H3N+-C- CH2 H3N+. H3N+-C- CH2 H2N+ H2C CH2 CH2 CH2 NH CH2 CH3 Methionine (M) Met Phenylalanine (F) Phe Tryptophan (W) Trp Proline (P) Pro Chooce a File HI HI
Give the 4 types of Biomolecules - their chemical composition, monomer, function/s, types and 2 examples for each type (1 example is for plants and the other example is for animals).
Choose the best response for each of the blanks in the statement below. When it is part of a polypeptide chain, proline is a known disruptor of [Select] because of [Select] [ Select ] its hydrophobic character the strain brought about by the five-membered ring the lack of an amino hydrogen in the backbone the lack of a freely moving side chain Select ] primary structure secondary structure tertiary structure quaternary structure
Analyze the following biomolecule using the criteria listed below. Be sure to be clear, concise, and complete with your responses. 1. What class of biomolecules does this compound belong to? Explain why. 2. Break this compound down into its components and clearly identify each section of the molecule by labelling (circle or draw an arrow to) its backbone structure, all functional groups, and all biomolecules in the structure. 00-P-O NH3 HO
Consider the tripeptide phenylalanylcysteyl methionine. Part: 0 / 2 Part 1 of 2 Draw the structure of this tripeptide at physiological pH. Click and drag to start drawing a structure. : ☐
697149&page%3D2 ning System (Academic) 49 When we refer to the backbone of a polypeptide, we are referring to the attachment between: Select one: out of O a. The amino, carboxyl group and the oa-carbon O b. The peptide bond between two amino groups question O c. The amino acids making the polypeptide O d. The amino and carboxyl groups only O e. The R groups of the amino acids Which of the following molecules is a polymer made from large number of building blocks called monomers linked together by covalent bonds? 50 out of Select one: O a. Glucocorticoids, a steroid hormone question O b. Waxes (such as beeswax) O c. Glycogen, that stored in liver cells O d. Cooking oils O e. Stearic acid (saturated fatty acids)
E. PROTEIN PRIMARY STRUCTURE ELUCIDATION. 1. Determine the primary structure of the protein described below. Write the final sequence using the corresponding three-letter code for each amino acid. Example: M-F-Y-R should be written as Met-Phe-Tyr-Arg Treatment with cyanogen bromide and sequencing yields the following peptide fragments: o D-M o R-A-Y-G-N o L-F-M Chymotrypsin digestion and sequencing yields the following peptide fragments: o G-N D-M-L-F o M-R-A-Y o o