BilayerleafletCOCOON1. Unfolded peptideaqueous phase2. Unfolded peptidein membrane3.α-helixin membraneFigure 1: Membrane binding peptide of a glycosyltransferase is shown interacting with amembrane. Positive charges are shown as blue +, negative charges are shown as red -.7. (3%)While the membrane binding peptide is in solution it is shown as being "un-folded" in Figure 1.(a) What is the name we give to this type of secondary structure? (Answerwith 1 sentence)(b) What is a general role of this type of secondary structure in a protein?Answer withproy

### 1. **Name of the Secondary Structure**: Random CoilThe term "random coil" refers to a…

Answered: Bilayer leaflet CO COON 1. Unfolded…

Organic Chemistry

9th Edition

ISBN:9781305080485

Author:John E. McMurry

Publisher:John E. McMurry

Chapter26: Biomolecules: Amino Acids, Peptides, And Proteins

Section26.SE: Something Extra

Problem 50AP: The -helical parts of myoglobin and other proteins stop whenever a proline residue is encountered in...

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I did not understand soultion for the question.. The relationship between Affinity and Association & Dissociation Constant. Four proteins (A-D) all bind the same ligand (X), with different affinities. For protein A & B we know that they have a binding site for X with a Kd (dissociation constant) of 10⁻⁵and 10⁻⁸ M, respectively. For protein C and D we know that they have a binding site for ligand X with a Ka (association constant) of 10³and 10⁵M, respectively. Which protein has the highest affinity for ligand ? Explain your reasoning. How do you make them all in same constant so that values can be compared and the one with highest Ka or lowest Kd (Highest affinity in both cases) can be ruled out.
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The following diagram illustrates the process of fragment-based drug discovery Đinding site her Sereen For tst ligand Sogen fer 2nd ligand Optimise Pretein Protein Protein A B. Optimise Link Pretein Protein Protein 14. What are the fragments labelled A and B known as? nhsioiyg onolisubiour a. Analogs b. Conformers c. Epitopes d. Pharmacophores afomya ado nol quoig 15. Which of the following statements is true? aloid s hoo bruage bb a, Parallel synthesis involves synthesis of a mixture of compounds in each reaction ves b. Parallel synthesis involves synthesis of a single compound in each reaction vessel c. Combinatorial synthesis involves synthesis of a single compound in each reaction w d. Parallel synthesis requires the use of a linker which must be cleaved at the end of badtode au of elist brucgnca a bias oilyxoctep sis ess1eriweulbre oviv niprif g ab 6. Which of the following is not a requirement for a linker used in solid phase synthesis beng nltas al a. The linker must be…
5 ased on molecular weights of purified (no beta-Me) and (beta-Me) sample, which are 97.4 kDa and 47.2 kDa, what can be said about the number and size of the protein monomers, as well as the nature of the bonds holding together the complete quaternary structure of the proteins?
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Shown below is a section of beta-sheet from the protein thioredoxin. Amide nitrogens are indicated by circled Ns, carbonyl oxygens by Os, and hydrogen bonds by gray lines. M strand 1 MO strand 3 (N) O 1 2 3 4 For each strand of the sheet (1, 2, 3, 4) indicate the direction (top or bottom) of the N-terminus. [Select] strand 2 [Select] O [Select] strand 4 [Select] strands 1 and 2 Determine the orientation (parallel or antiparallel) of each adjacent strand to one another. [ Select] AHO strands 2 and 3 [Select] N strands 3 and 4 [Select] >
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macollege.instructure.com/courses/352/pages/covid-proteins-lab-manual?module_item_id=D44333 A = abc Where "A" is absorbance, "a" is molar absorptivity, "b" is the path length (length of the cuvette in units of cm), and "c" is concentration (mol/L). The molar absorptivity is an intrinsic property of a molecule which tells us how intensely it will absorb at a particular wavelength. If "A" is a unitless quantity, "b" is in units of cm, and "c" is in units of mol/L, then what are the units of molar absorptivity? Do a little research to learn how alpha-helices and beta-sheets are drawn in protein structures. If most of the absorption properties are coming from the alpha-helices in these proteins, and many alpha-helices have similar absorbance properties across different proteins, which protein would you predict would have the highest molar absorptivity? Your job is to use the following data table to determine the molar absorptivity for each of the following proteins at their respective…
Question 2. While internal cysteine amino acid sidechains in proteins undergo oxidation to produce disulfide crosslinks that stabilize the protein structure after folding, solvent-exposed cysteine sidechains can remain in their reduced thiol form and serve as reactive nucleophiles (recall for instance Acyl Carrier Proteins involved in fatty acid biosynthesis or various oxidoreductase enzymes). The reactive thiol groups in proteins can be detected using Ellman's test, wherein the protein is reacted with a disulfide Ellman's reagent to form a new mixed disulfide and a 2-nitro-5-thiobenzoate (TNB) byproduct. Upon addition of base, TNB is deprotonated to form a dianion, which absorbs light in the visible region and can be detected using UV-Vis spectroscopy. Ellman's Reagent CO₂H -NO₂ internal disulfide crosslink O₂N- HO₂C SH solvent- exposed thiol UV Absorbance at 412 nm O₂N- -S TNB²- alkaline pH O₂N- SH HO₂C 2-nitro-5-thiobenzoate (TNB) -NO2 mixed disulfide CO₂H a) Provide a detailed…
What is the isoelectric point (pl) of arginine? Relevant amino acid structure is shown below: pka RCO2H/NH3*/other O 10.76 5.61 O 7.33 O 7.00 2.54 H3N-CH-C-OH CH₂ CH₂ CH₂ Please click here if image does not display correctly. 010 NH C=NH2 NH₂ Arginine Arg 2.17/9.04/12.48

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