1. If Ser 80 was replaced with Arg what kind is the change in the bond type between these two molecules? Will this change be more or less stable. Explain 55NH Thr 55Ser 5254NHO-Thr 53NHP-CH₂-CO_ Arg HCH105,Ser80Lys:84His 134AdjacentchainArg 167CH₂Arg229Gin231

the stability of an amino acid is influenced by the specific interactions it forms with other amino…

Answered: 1. If Ser 80 was replaced with Arg what…

1. If Ser 80 was replaced with Arg what kind is the change in the bond type between these two molecules? Will this change be more or less stable. Explain

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

See similar textbooks

Similar questions

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?
12. The sugars glucose, fructose, and inositol all have the same formula i.e. C6H12O6 yet they have 3 very similar but different structures. This is an example of: a) geometric isomers b) structural isomers c) stereo isomers d) none are correct
19.
1) Find the pH of 0.1 M of the differnet forms histidine species. (See image for equation and pKa values) 2) What is the principal specis at pH 1, pH 5, pH 8, and pH 11?
1. Most globular proteins are denatured and lose their activity when briefly heated to 65°C. However, globular proteins that contain multiple disulfide bonds often must be heated longer and at higher temperatures to denature them. Furthermore, upon cooling of the denatured proteins, the activity of these proteins can often be restored. Explain these properties.
2. Consider the following quaternary cartoon structure below, where each colored shape represents a different subunit. i. ii. iii. How many N-termini are there in this complex? Suppose the blue square and orange triangle subunit are held together by a disulfide bond, sketch below what you would expect to see after the addition of BME. What kind of interactions may be responsible for holding the orange triangle and green circle subunits together? List at least three.
1. The following protein crystal structure is the Human Serum Albumin complexed with octadecanoic acid (PDB ID: 1E7I). According to the protein data bank, Human Serum Albumin is composed of 72% helical structure. Among the following options (a-c), select the possible Ramachandran plot for the above Human Serum Albumin. (a) (b) (c) Phi Phi Phi
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.
Describe why G-C bonding is stronger than A-T. Why is it important?
3. Which best describes the contribution of tertiary (3’) structure of to the native conformation of polypeptides and proteins: a) Structure that results from intrachain interactions of amino acid side chains b) Structure that results from interchain interactions of amino acid side chains c) Structure that results from base pairing d) Structure that results from the linear sequence of amino acids from beginning to end of molecule