4. Gamma turns are divided into two classes based on the phi and psi rotationalbond angles of the residue at positions n + 1. In the classical gamma turn, theresidue at position n + 1 has phi = + 70 degrees and psi = -60 degrees, whereasin the inverse gamma turn, the residue at position n + 1 has phi = - 70 degreesand psi = + 60 degrees. Draw a Ramachandran plot and indicate the location ofthese bond angles on your plot.

An illustration of the permitted and forbidden areas of the phi and psi dihedral angles in the…

Answered: Gamma turns are divided into two…

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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Each group will be provided with 20 g double-stranded DNA oligomer in STE buffer (0.1M NaCl/ Tris/ 10 mM EDTA, pH 7.4). The sequence of one strand of the oligomer is: 5’-AATGGTACGTATACTTTAT-3’ - show a table of % denaturation of DNA at different temperatures, using the equation provided in “Calculation” - plot a graph of % denaturation of DNA vs different temperatures with clear label and title, and hence determine the experimental Tm of the DNA sample - calculate the theoretical Tm of the sample using Marmur and Doty equation, compare the experimental Tm with theoretical Tm of the DNA sample
In a gel electropherosis, Glutamate and valine created a double bond. How is that possible?
b) Consider the following experimental results: Total hydrolysis of a nonapeptide gave: Ala,Arg,Glu,Leu,Lys,Met,Phe,Tyr, Val One fragment from CNBr treatment was: Tyr-Leu-Lys One fragment from Chymotrypsin treatment was Arg-Glu-Met-Tyr One fragment from Trypsin treatment was Val-Ala-Phe-Arg ii. The reagent shown below is widely utilized in the sequencing of peptides. Treatment of the nonapeptide you deduced in part i. with this reagent yields a phenylthiohydantoin derivative, compound 1, and an octapeptide. Write a mechanism for the formation of compound 1. N=c=8
why 3 methyl histidine is used to measure muscle mass?
a and b please
Please answer the following questions 1) based on the structures of adenine, cytosine, guanine, and thyme. Why does A prefer to bind to T and C prefer to bind to G 2) were the binding energies the same for AT and CG? Explain the difference 3) which of the four know bases is the unknown synthetic base most like in terms of its binding characteristics? What does this indicate about its structure? 4) if the unknown synthetic base was used to study DNA replication, which natural bases would it interact with? 5) is the picture question
An organic chemist is generally happy with 95% yields. If you synthesized a polypeptide and realized a 95% yield with each amino acid residue added, what would be your overall yield after adding 10 residues (to the first amino acid)? After adding 50 residues? After 100 residues? Would these low yields be biochemically “satisfactory”? How are low yields avoided, biochemically?
Please identify the following on the Michaelis- Menten plot shown A, B, C, and the X and Y axes. Please briefly explain the significance of each. A B с
what is the correct method for protien purification if the PI of three protiens are: protien 1: PI= 6.25 Protien 2: PI= 6 Protien 3: 10.5 all the protiens are Positive
The melting curve for the polyribonucleotide poly(A) is shown below. (a) Explain why absorbance increases with increasing temperature. (b) Why does the shape of the curve differ from the one shown in Fig. ?
This SDS-PAGE loading buffer has SDS (a denaturing detergent), β-mercaptoethanol (a reducing agent), Coomassie Blue (a dye), and glycerol. You will need to dilute your protein samples such that the final concentration of the loading buffer is 1x, meaning that you will add 5 parts of the protein sample for every 1 part of 6x buffer. Calculate how much of the 6x loading buffer you will need to add to each sample. Then, add the appropriate amount of 6x SDS-PAGE loading buffer to the samples. Store the samples in the -20°C freezer. What is the final concentration of glycerol in each of the samples?

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