1. Cirde and identify three different functional groups on the following diagram OH 1. 2. 3.
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![I Or 7
1.
Circde and identify three different functional groups on the following diagram
HO.
H3C
1.
2.
3.
2.
State a possible function of each indicated cell part below:
H-I](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F11c08268-409d-4492-b844-51aebb83c26d%2F58f4d44e-1bde-4a3c-ac87-a5f199125af6%2F247admq_processed.jpeg&w=3840&q=75)
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- 6:18 < BCH351_Assignment... 6.1. The graph below shows the fluidity of liposomes composed from 4 different phospholipid bilayers. Melting curve 'a' corresponds to a membrane composed of phosphatidate linked with hexadecanoate fatty acids. The melting temperature, Tm, for that membrane is indicated on the graph as a dotted vertical line. At temperatures below the Tm, the membrane becomes more gel-like and much less fluid than above the Tm. Curve b) The compositions of the other 3 liposomes are listed below (numbered 1-3). Match the liposome compositions to the different melting curves (labeled 'b', 'c' and 'd' on the graph). Explain your answers. 1) Phosphatidate composed of octadecanoate fatty acids 2) Phosphatidate composed of hexadecanoate fatty acids + cholesterol 3) Phosphatidate composed of 16:1cA³ fatty acids Curve c) 3 Curve d) Fluidity 5G UC.ll 90% a B Tm Temperature :blank 1 T or R blank 2 low or high oxygen affinity blank 3 planar or domed blank 4 oxygenated or deoxygenated blank 5 perpendicular or not perperndicular blank 6 wide or narrowHelp please! I am stuck!
- Number 630. The cooperative binding behavior of hemoglobin for oxygen is best explained by... Group of answer choices The movement of the proximal histidine upon O2 binding causes a structural change at the binding interface between subunits The oxidation of Fe2+ to Fe3+ and formation of the superoxide ion causes distortion of the protoporphyrin ring, altering binding interface between subunits The tetrameric nature of hemoglobin's quaternary structure directly confers cooperative binding activity The movement of the distal histidine upon O2 binding causes a structural change at the binding interface between subunits The binding of O2 causes a pH shift that changes the protonation state of amino acids located at the interface between subunits The solubility of hemoglobin in aqueous solution and its insolubility in nonpolar environments13. 0.9% (m/v) NaCI solution and 5% (m/v) glucose solution are both isotonic to red blood cells. SHOW your work and watch sig figs & units. c. convert the concentration from M to % (m/v) for a 0.342 M NaC solution. (HINT: convert to g/ml and then multiple by 100%)
- 2B. S. aureus hemolysin B attacks the RBC cell membrane by hydrolyzing the sphingomyelin headgroup: ОН HN .R hemolysin B cuts this bond i) Draw a plausible mechanism of hydrolysis for this lipid headgroup. Let B- and BH be general base and general acid. 00-P-O LOR2 OR, ii) Why is this damaging to the overall membrane architecture of the RBC?8L.3.4.1 Given structures (Betaxlol) and (Timolol), which one would be a better choice topically to treat glaucoma in a patient with a history of asthma? Provide a SBTE for your answer. cr 0- CH2-CH-CH2-NH2-CH(CH3)2 -H2C-0-H2C-H2C- ÓH (Betaxolol) -00, c=C, H H -o-CH2-CH-CH2-NH2-C(CH3)3 (Timolol) OH
- 2. (a) The binding site of 2,3-bisphosphoglycerate (BPG) (red stick figure) in the deoxyhemo- globin molecule is illustrated below. Note that the two phosphate groups and the carboxylate group of the BPG molecule confer strong, negative electrostatic character to the molecule. B₁-subunit 1. 2. 3. 5. 6. B₁ (b) Mutant Hemoglobin Hb Raleigh Hb Helsinki The mutant hemoglobins listed below each have a mutant amino acid in the ß-subunit directly in or in the vicinity of the BPG binding site. Rank the affinity of the following mutant hemoglobins for binding BPG (red stick figure above).. Explain your reasoning. The notation, for instance, as given for Hb Raleigh Val(31)Ala means that Val-1, the first amino acid residue of the ß-subunit, has been substituted by Ala. Hb Rahere Hb Rancho Mirage Hb Little Rock B₂ Hb Ohio Mutation Val (31)Ala Lys(382) Met Lys(382)) Thr His(143)Asp His(3143)Gln a-NHẠ Ala(142)Asp His 2 His 143 BPG His 143 Lys 82 His 2 Rank the affinity of the mutant hemoglobins for…If normal plasma pH is 7.4 and normal [CO2) is 1.2 mM, what is the normal (HCO321? The pK9 for this system is 6.1. Phosphoric acid (H3PO4) has three dissociable protons, with the pK,'s shown below. Which form of phosphoric acid predominates in a solution at pH 4? Explain your answer. Acid H3POA 2.14 H2PO4 6.86 HPO,2- 12.4Sketch the appearance after visualization of a protein mixture containing the seven proteins (ovalbumin, insulin, fibrinogen, y-globulin, collagen, hemoglobin, myoglobin when subjected to isoelectric focusing
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