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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A 1.00-mg sample of a pure protein yielded on hydrolysis 0.0165 mg of leucine and 0.0248 mg of isoleucine. What is the minimum possible molar mass of the protein? (MMleucine=MMisoleucine=131g/mol)
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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?
How would I calculate the isoelectric point for a peptide (LSGHKKRDDQ) that has zwitter ion after 9.60 and -2 charge after 10.53 ?
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] >
1. Please describee (1) Type I B-Turn and (2) Type II B-Turn in detail. 2. Please show a protein structure which contains a "TIM beta/alpha-barrel fold domain". (20%) 3. Please show a protein structure which contains a "Canonical Rossmann fold domain". (20%) Please show a protein structure which contains a "Immunoglobulin-like beta-sandwich fold domain". (20%) 4.
Shown below is the amino acid tyrosine in its protonated state, with the pK₂of each ionizable proton indicated. pK₂ = 10 HO COOH pk = 9 pK₂ = 2 Which best represents the predominant state of tyrosine at pH 7? a HO. O O OO a b U H3N P H₂N COOH b H₂N COO с НО. H₂N COO d HO. H₂N COO
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…
Isoelectric focusing can separate peptides based on their relative contents of acidic and basic residues. When voltage is applied to an electrophoretic gel with Amino acid pK Arg 12.5 a pH gradient, each peptide migrates until it reaches a point where it has no net charge. The pH at this point is the isoelectric point (pl) for that peptide. Asp 3.7 Cys 8.2 One can estimate the pl fairly accurately (within 0.1 or 0.2 pH units) using the Glu 4.3 pK values of all the proton dissociable groups in the peptide. His 6.0 Consider the hexapeptide Met-Asp-Lys-Arg-Ala-Tyr. Lys 10.5 Tyr 10.5 *peptide-NH; 8.0 *peptide-COOH 3.4 * Amino and carboxy terminal values differ from the a amino and carboxy values of a single amino acid. Step 1: Determine the total positive charge on the hexapeptide when all acidic and basic groups are fully charge: protonated. Enter your answer without the sign.
Could someone explain what this is saying? I would like a better understanding. FIGURE D CPP32 (Caspase-3) protease activity. Aliquots of cell lysates (50μL) were incubated with an equal volume (50 μL) of the reactionbuffer and 5 μL of 7-amino-4-trifluoromethyl coumarin (AFCDEVD) for 1 hour at 37˚C (Clontech). The shift in fluorescenceemission of AFC-DEVD, on its proteolysis to free AFC by theprotease, was detected in a fluorometer, using a 400 nm excitationfilter and 505 nm emission filter.
The Hill coefficient (nH) for myoglobin is_; whereas for hemoglobin nH is about _. O 2.8; 5.0 O 1.0; 2.8 2.8; 1.0 O 5.0; 2.8

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