100%"iew History Bookmarks ProfilesTab WindowHelpL 1.7 En: XPeriod x G how de XG compe xA HIP 40 x MeA Bioche XEnzym xO How E Xhillis2e xOle.com/document/d/1hnoCPOrL39Y-u9G8IsygmuPu--OL3T8QnHVAAZEmuQo/editO What is a Protein?.Macromolecules [. Structure- Chamberlain and. a indivchapter7.pdf. E 1.4- Understandin.O How to unboil an.nemistry Quiz #2: Macromolecules & Enzymes (Brosseau)Request edit accesspols Help3. What is the name of the molecule in thecircled region labelled M (be specific)? Howdo you know? (1)4. Explain the difference between the"chemical bonds" labelled L and N in thediagram and the importance of each to thestructure of this molecule. (2)HHOH HO5. Draw a diagram to show how themonomers to the right could be joined toform a polymer and identify the name ofthe linkage. (2)H-N-C-C-OH + H-N-C-C -0-HCH36. Name this macromolecule. Be specific. (0.5)7. Identify the type of bond in the circle. (0.5)A8. Explain how the structure of this moleculemakes it well suited to its function. (2)10AaMacBookCRook AirDDF2F6F7FIOF11%23$4&34.6.7.1W-T.YP.< CO

The backbone of a nucleic acid is made up of a sugar-phosphate chain linked by phosphodiester…

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Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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og g ad peptide bond Primary Structure Secondary Structure PH- CH og CH CH HC LCH HỘ HÈ HỒ LỊCH Tertiary Structure CH NH3+ CH-S- CH € Quaternary Structure 2. Using the images above: a. What bond types occur in the secondary structure of a protein? b. What bond types occur in the tertiary structure of a protein? c. What bond types occur in the quaternary structure of a protein?
6. Using the charges you calculated above, plot the characteristics of alanine over a range of pH values. Connect the points by estimating what the charge should be at pH values where you lack data. It is possible to calculate the charge at any pH, but if you understand the relationships presented here you will be able to make estimates quickly and easily. +2 +1.5 +1 - +0.5- -0.5 - -1- -1.5 - 7. 6. 11 13 14 pH of solution 7. Aspartic acid has a side chain bearing a carboxylic acid group; its pK, is 4. The a-amino and a-carboxylic groups have pKa values similar to those of alanine. Determine the net charge on aspartic acid at the following pH values: pH 1 pH 2 pH 4 pH 9 pH 13 Net charge of molecules 2.
1. Hypoxanthine is an unusual nitrogenous base that can be formed from adenosine; it is not normally found in nucleic acids. Hypoxanthine has a single ionizable group with a pKa of 8.7. If you dissolved hypoxanthine in an aqueous solution at pH 7.0, would this ionizable group be protonated or deprotonated?
Draw the structure of the 06-methyguanine:protonated cytosine base pair (three hydrogen bonds form between the two bases). Use bond Any to draw hydrogen bonds. CH3 N- N- R R 'N. H
Please answer all parts with explanations. This is biochemistry
Φ and ψ in the Ramachandran plot (below) are: a) Rotational angles around the bond between the α-carbon and N-H (Φ) and C=O (ψ). b) Amino acid solubility in octanol (Φ) and water (ψ). c) Hydrogen bond angles in α-helices (Φ) and β-sheets (ψ). d) Amino acid solubility in water (Φ) and octanol (ψ).
8. NMR measurements have shown that poly-lysine is a random coil at pH 7 but becomes a helix when the pH is raised above 10. If the same type of folding behavior is observed, what should be the pH dependence of poly-glutamate? A) Helix at pH 7 but random coil at pH 10 B) Random coil at pH 3 but helix at pH 7 C) Random coil at pH 7 but helix at pH 10 D) Helix at pH 3 but random coil at pH 7
3. The following structures are the components of nucleic acid. CH2OH ОН NH2 ОН ОН A (a) Which type of base is the molecule B? (b) Is molecule A be found in DNA or RNA? Explain. (c) Draw a nucleoside using the appropriate structures provided above. While drawing the structure, also consider the conformation. 7 (d)What are the differences between the structure of dATP from the structure vou draw in (c)? (e) Fill in the blanks for the relative percentage of bases in a DNA. А G T 13 15 Strand 1 12 Strand 2
2. You made a pH=2.5 buffer solution by mixing NaOH and glycine to give a solution that is 0.20 M in total concentration of glycine. (pka1=2.34 and pka2=9.69) a) What 2 glycine species are present in the buffer solution at this pH? (draw their structures) b) What is the concentration ratio of these 2 species? c) How many moles of each species, A- and HA, is there in 500 ml of the buffer solution. d) If 25 ml of 0.82 M HCI is added to 500 ml of this buffer solution. What reaction is taking place? What is the final pH of the solution? Is the solution still a buffer? e) Draw the titration curve, pH versus equivalents of OH-, for glycine and determine the pl.
You have been so enamored with lab during your time in Biol201 that you decide to do some biology research yourself over summer break. You discover that the single macromolecule shown below is found in Piggy's skin. 1. What type of macromolecule is shown? a. Name the level of organization of the overall structure. b. Name the secondary structure(s) visible. c. Name the bond holding together the monomers of this structure. d. What effect would a silent mutation have on the shape of this structure?
9. a) Nucleic acids, proteins, and polysaccharides all share a similar structure. How is the structure of lipids different from these macromolecules?
1.Describe in detail how to detect the primary structure of protein. 2.Given a mixture of lysine,histidine and cysteine.The isoelectronic point of the amino acids are as follows: histidine:7.64 lysine:9.74 cysteine:5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.

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