vas seconds ago E E Image options Replace image- . 4 6. A protein molecule composed of a sequence of polar amino acids, shown in blue, and a sequence of nonpolar amino acids, shown in pink is shown schematically below. How might you expect this protein to be located in the several phospholipid structures shown below? Choose all reasonable structures. 田回 !!!

vas seconds ago E E Image options Replace image- . 4 6. A protein molecule composed of a sequence of polar amino acids, shown in blue, and a sequence of nonpolar amino acids, shown in pink is shown schematically below. How might you expect this protein to be located in the several phospholipid structures shown below? Choose all reasonable structures. 田回 !!!

Chemistry: Principles and Reactions

8th Edition

ISBN:9781305079373

Author:William L. Masterton, Cecile N. Hurley

Publisher:William L. Masterton, Cecile N. Hurley

Chapter23: Organic Polymers, Natural And Synthetic

Section: Chapter Questions

Problem 44QAP: A 1.00-mg sample of a pure protein yielded on hydrolysis 0.0165 mg of leucine and 0.0248 mg of...

See similar textbooks

Similar questions

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…
kamote tops juice Clear selection In this reaction below, the conjugate base of ethanoic acid is H3C-C O-H H20 H3C-C H30 Н20 H30+ CH3COO- CH3COOH Benedict's reagent is used as a test for the presence of reducing sugars. Molisch test Benedict's test Barfood'o Tast
6, The structure originelly proposed For Cordycepic acid, [a] +40.3°, has been + 40.3°, has been shown to be in Correct, suggest to be reason skeptical obout the original Structure, which is given below CO2H 1.29 HO HO.
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…
8. The following proteins represent a wide range of molecular weights and isoelectric points. Mr is the molecular weight of a single protein chain. • Protein 1: Mr 68,544; pl 6.11 (monomer) • Protein 2: Mr 29,041; pl 5.32 (dimer) • Protein 3: Mr 15,805; pl 5.7 (dimer) • Protein 4: Mr 12,165; pl 4.74 a. Which protein is the most acidic? Explain your answer. b. Which protein will migrate the slowest in an SDS-PAGE? Explain your answer. c. In what order will these proteins elute from a cation exchanger at pH 8? Explain your answer. d. In what order will these proteins salt out from a pH 7 solution by the dropwise addition of saturated ammonium sulfate? Explain your answer. 5 83°F Cloudy
ogical Marcomalee Identifying specific interactions between residues in a protein Imagine the main chain of a protein bends back on itself, so that two amino acid residues R, and R, come close to each other. Here's what R, looks like: -CH- -- CH2 OH O yes Could R, form a hydrogen bond with R₂ at physiological pH, if R₂ were the right kind of residue? O no If you said R, could form a hydrogen bond with R2, what would R₂ have to be? If there's only one possibility, write its 3-letter code. If there is more than one possibility, write the 3-letter code of any of them. 0 Explanation Check ㅎ C S A * 2 # 3 $ 4 Z W M S X Ő % Λ 25 & 6 7 E R T Y U D C dill LLC. All Rights Reserved. Terms of Use Privacy Center NP 8 A 9 O 0 LL F G H J K L V B N M P alt
What is the ratio of CATION to ANION in Drug X? [blank1] H₂C -H Fogy CH3 SO42 'N CH3 Drug X CH3NH Describe the possible interactions between the SIDE CHAINS of amino acids: I. and II.... II. and III... I. and III... 1. COO NH3* 2 HO II. COO HO NH3* COO NH3* III.
9. Which of the following non-covalent interactions could the sidechain of F266 participate in. Place an "X" next to all that apply. lonic (or salt bridge or charge-charge) Hydrogen bond Dipole-dipole Dipole-induced dipole Induced dipole-induced dipole Charge-dipole Charge-induced dipole П-stacking 10. The thermodynamic values for the folding of a protein are as follows: AG° = -38 kJ/mol = AH° = -164 kJ/mol AS -0.68 kJ/K.mol Which one of the following statements is most likely true? Circle your answer. A. Folding of this protein is primarily driven by the formation of favorable noncovalent interactions in the folded protein. B. Folding of this protein is primarily driven by the formation of hydrogen bonds between the protein and the bulk solvent (water). C. Folding of this protein is primarily driven by the loss of conformational entropy in the folded protein. D. Folding of this protein is primarily driven by the gain of conformational entropy in the folded protein. E. Folding of this…
The above amino acid, shown at pH = 7.0 and where every atom (including hydrogens!) is visible, is (D or L) -X-
A. Amino Acids with Electrically Charged Side Chains Negative Pesitive Aspartie Acid Glutamie Acid (Asp D Lysine Histidine Arginine (Argl ® (Glul O (His H HO Ho HO -NH, -NH, NH, NH, -NH, NH NH H,N- ONH, ONH, C. Special Cases B. Amino Acids with Polar Uncharged Side Chains Proline Asparagine (Aan N Cysteine (Cya) © Glycine (Gly O Threonine Glutamine (Pra) P Serine (Ser 9 Но Họ Ho Ho Ho Но NH, NH, NH NH, NH, NH, -NH, но- SH он NH, NH, D. Amino Acids with Hydrophobic Side Chains Leucine (Leu O Phenylalanine (Phe e Tryptophan (Tp W Tyrosine Methionine Valine Isoleucine Alanine (Ala A IMe M Ho Ho Ho Ho HO NH, -NH, Но -NH, HO NH, NH, NH, NH, NH, NH он If the chromatogram was developed from reverse phase conditions, which of the following amino acids is expected to elute first? serine phenylalanine tryptophan O tyrosine
4: Draw structures from notations or notations from structures, for the following dipeptides. Look up in book for the structures of various amino acids and their names (and notations). (EOCQ 60) Hints for drawing a dipeptide from the specified amino acids. From the given symbols (Ser, Thr, etc), draw the structures for the amino acids in the specified order example, for Ser-Thr, draw Serine first and then Threonine). Then remove the OH from the first amin and one H (from the N atom) on the second amino acid. Then join the remaining fragments; that give the dipeptide formed. In these reactions, H2O is formed as a side product; but it is implied, and you have to show it in your answers. The following equation illustrates that. Here, R and R' are symbolic. In an actual question, you must the actual structures for the amino acids (Table 16.3 in the book). O H || | Н.N— CH— С-N-CH—С-ОН H,N-CH-C–OH + H,N-CH-Ċ–OH R' R. R' (H2O is a sid no need t Amino acid 2 dipeptide Amino acid 1 а. Cys-Ser…
Although the bond energy for the hydrogen bond in a vacuum is estimated to be about 20 kJ/mol, we find that each hydrogen bond in a folded protein contributes much less--probably less that 5 kJ/mol--to the enthalpy of protein stabilization. Suggest an explanation for this difference. Explain briefly.