Question 4. Imagine the main chain of a protein bendsback on itself so that two amino acid residues R1 and R2come close to each other.In the table below are four possibilities for what R1 andR2 might be. In each case, decide whether a specificinteraction could form between the residues. If a specificinteraction could form, give the name of the interaction.R₁cysteinetyrosinethreoninearginineR₂cysteinephenylalanineglutamineaspartatespecificinteraction?OOyesO yesO nonoOOO yesnoyesnoname of specificinteraction0П00

There are four classes of biological macromolecules: proteins, nucleic acid, lipids and…

Answered: Question 4. Imagine the main chain of a…

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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You have discovered a new amino acid that you name in honor of your favorite course. Twofourteeninine has an alpha-amino and an alpha-carboxylic group, and an ionizable side chain that carries an amino group. A titration curve of twofourteeninine is shown below. Net charge a P I 1 2 I 3 4 5 6 pH T 9 10 11 12 13 What are the approximate pKa values of twofourteeninine (to the nearest half-pH unit)? Check all that apply.
Draw the amino acid below in its most protonated form, any intermediately protonated forms, and its least protonated form. Also draw a titration curve for this amino acid, with pH on the y-axis and equivalents on the x-axis going from acidic to basic (most protonated to least protonated) using the pka values below. Match the protonated/deprotonated forms to the appropriate regions of the titration curve. Scan your drawing, and upload as a pdf, jpeg, or tiff file. H3C O NH₂ pKas are provided below: OH
Components of Complex Biomolecules Figure 1-10 (Lehninger's Biochemistry book) shows the major components of complex biomolecules. For each of the two important biomolecules below (shown in their ionized forms at physiological pH), identify the constituents. And show H-bonding with water. (a) Guanosine triphosphate (GTP), an energy-rich nucleotide that serves as a precursor to RNA: N- NH -CH2 0- NH2 H H H H. ОН ОН (b) Phosphatidylcholine, a component of many membranes: CH3 O- CH3*N-CH2-CH2-0-P-0–CH2 нн CH3 НС —О—С—(CH), —С—С— (CH), — СHз CH,–0-C-(CH,)14–CH3
Proteins, the building blocks of life, have several functions in the human body and all the operations depend upon the structural specificity which can be explained by the lock and key hypothesis. Expand the idea
I'm working on the thermodynamics of protein binding but I want to understand more on the enthalpic and entropic components of a binding reaction. Could you please explain?
i. ii. i.v. 22. Using the figure below, answer the following questions. Identify 2 independent helices domains Identify a disordered region In the structure, box the cofactor and name it (abbreviation accepted) Using the figure, draw the structure of the cofactor bound to this protein
I need the answer as soon as possible
The drop-down answers choices for questions 1 through 4 are NH3, COOH, CH2, or OH. The drop-down answers choices for questions 5 through 6 are negative, neutral but polar, neutral and hydrophobic, or positive. The drop-down answer choices for question 7 is a picture attached below.
QUATERNARY STRUCTURE One final level of structure exists for some, but not all, proteins. This is called quaternary structure. Proteins that have quaternary structure are formed from two or more polypeptides that assemble into one active structure. The different polypeptides in a protein with quaternary structure are often called subunits. These subunits may be identical or different. One example of a protein with quaternary structure is hemoglobin, the protein that transports oxygen in our blood. The structure of hemoglobin is shown in Figure 8. B- Fe2+ Heme a Figure 8. Quaternary structure of hemoglobin with labeled subunits. Note: each subunit contains one non-protein heme group complexed to an oxidized iron atom (Fe2+). These “prosthetic groups" are required for carrying oxygen in the blood. Modified from this link under Creative Commons license. Answer the below questions on quaternary structure in your own document. 1. Based on your interpretation of Figure 9, how many subunits…
Part B Assume a protein is composed of 120 amino acid residues and that each amino acid can have three possible orientations. How many total possible orientations are there for the protein? Express the number of possible orientations to three significant figures. —| ΑΣΦ 1.797 • 1057 Each possible orientation of an amino acid is due to rotation about a bond. Since there are two terminal amino acids, there will be one fewer peptide bond compared to the number of amino acids. No credit lost. Try again. Submit ? Previous Answers Request Answer orientations
Figure 7 shows one additional type of bond that can stabilize the tertiary structure of a protein. This bond is called a disulfide bond (or disulfide bridge), and it involves the sulfhydryl (-SH) R groups from one particular type of amino acid. A disulfide bond can form only under certain conditions (oxidative conditions). We'll talk about oxidation and reduction next week. For now, just note that this type of bond does exist in some proteins. Answer the below questions on tertiary structure in your own document. 8. Figure 6 shows examples of bonds that might stabilize the tertiary structure of a protein (labeled A, B, and C). Do these interactions involve only the amino acid R groups, only the polypeptide backbone atoms, or both? 9. In the table below, indicate what type of bond/ interaction is represented in the examples shown in Figure 6, panels A, B, and C and whether each interaction involves group or backbone atoms. Example Type of Bonding Interaction R group or backbone? A В 10.…
In terms of structure and function of a protein why is the lactase enzyme have a optimal pH of seven

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