Which factor contributes to the selectivity pore of the potassium channel from S. lividans? O backbone carbonyl groups in irregular secondary structures O negatively charged amino acids near the channel opening O the N-terminal ends of 4 a helices O both backbone carbonyl groups in irregular secondary structures and negatively charged amino acids near the channel opening O both backbone carbonyl groups in irregular secondary structures and the N-terminal ends of 4 a helices

Which factor contributes to the selectivity pore of the potassium channel from S. lividans? O backbone carbonyl groups in irregular secondary structures O negatively charged amino acids near the channel opening O the N-terminal ends of 4 a helices O both backbone carbonyl groups in irregular secondary structures and negatively charged amino acids near the channel opening O both backbone carbonyl groups in irregular secondary structures and the N-terminal ends of 4 a helices

Biology: The Unity and Diversity of Life (MindTap Course List)

15th Edition

ISBN:9781337408332

Author:Cecie Starr, Ralph Taggart, Christine Evers, Lisa Starr

Publisher:Cecie Starr, Ralph Taggart, Christine Evers, Lisa Starr

Chapter39: Digestion And Nutrition

Section: Chapter Questions

Problem 4CT: Cholera is a disease caused by bacteria that make cholera toxin. In the presence of this toxin,...

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(c) The tube and cylinder diagram to the right illus- trates schematically the potassium channel protein from a bacterium. This channel protein consists of four identical polypeptide chains each comprised of 119 residues. The cyan ribbon illustrates only two of the polypeptide chains. The relative positions of 4 α-helices, one from each poly- peptide chain, are shown as cylinders. The red sphere in the central part of the diagram shows the position of a potas- sium ion identified by X-ray structure analysis. A cesium ion (green sphere) was also found to be stabilized in the same position when cesium chloride was introduced into the crys- tals. The cylinders each represent an α-helix running from Tyr62 to Thr74. Considering the position of the potassium ion, in- dicate on one of the cylinders at which end of the cylinder residue Tyr62 is found and at which end residue Thr74 is found. Explain the basis of your answer? Ala23 Thr119 (d) The N- and C-terminal residues of one of the…
at punctures the bacterial cell wall has just been recently isolated from the F the peptide reveals the following information below: IOTE: when the sequence is nat knawn, a comma separates the amino acids) Hydrazine Acid Hydrolysis (6 N HCI) at 110 °C Heptapeptide (2) Arg, Pro, Phe, Tyr, Ala, Lys 2.4-dinitrofluorobenzene DNP-Phe Lys and modified free Peptide 1 (Ala, Lys) amino acids Cleovoge with Trypsin, then chromatography Peptide 2 (Pro, Arg, Tyr) Peptide 3 (Phe, Arg) Phe Cleavage with Chymotrypsin, then chromatography Peptide 4 (Arg, Tyr) Peptide 5 (Lys, Pro, Ala, Arg) When answering the questions below, please use the ONE-LETTER CODE for the amino acid, with NO spaces and symbols between each letter. 1. What is the C-terminal residue? K 2. What is the N-terminal residue? F 3. What is the sequence of Peptide 3? GP 4. What is the sequence of Peptide 5? LPAA 5. What is the averall amino acid sequence? AL
stion 2 Proteoglycans form proteoglycan aggregates after being bound to: vet answered Select one: Ked out of 1.00 O a. Glycogenin through a protein linker ag question O b. Glucourouic acid though a link protein O c. hyaluronic acid through an ionic attraction force stabilized by a link protein O d. Chondronic acid through a link protein NEXT PAGE
Consider the positively charged amino acid lysine Lys2+ 21 COOH I H&N-C-H I pH 14 12 10 8 6 4 2 0 CH₂ I CH₂ I CH₂ I CH₂ T NH₂+ 0 Nelson p85 2.18 = 2.18 PK₁ Lys+ COO™ I H₂N-C-H H₂N-C-H ī I -----) 8.95 Lysº 8.95 pK₂ pka carboxyl = 2.19 pkaamino = 9.67 pka sidechain = 4.25 COO™ I CH₂ I CH₂ I CH₂ I CH₂ I NH₂¹ 1.0 2.0 Equivalents of OH added- COO™ I H₂N-C-H I 10.79 1 10.79 pk Isoelectric point Lys CH₂2 I CH₂ I CH₂ I CH₂ T NH₂ 3.0 +H3N NH3+ T CH₂ T CH₂ CH₂ CH₂ -COO™ H Lysine (Lys, K) Physiological pH = 7.4 < pl → Amino acid is positively charged at physiological pH 1. Consider glutamate in its fully protonated form (e.g. in a pH = 1 solution) 1) Draw all the forms of glutamate at various pH 2) Calculate the pl of this amino acid 3) Sketch a titration curve showing pH as a function of added [OH-] and locate the predominant forms of histidine in the curve STEPS: 1. Find the H atoms that can be removed on the molecule 2. Associated a pka value to each removable H. 3. Draw the Aa structure at:…
Protease enzymes cleave proteins by hydrolyzing peptide bonds. The strategy for each type of metalloprotease begins with generating a nucleophile that attacks the peptide bond that attacks the peptide carbonyl group. O Macmillan Learning On the basis of the information provided in the figure, show the next step in the mechanism for peptide-bond cleavage by a metalloprotease. Metalloproteases H R₁ HN Zn Enz 2+ R₂ Draw curved arrows on the pre-drawn structures to show the metalloprotease mechanism. If you need to reset the structures, click More followed by Reset Drawing. Select Draw Templates Groups More B - H Enz H H с R1 | : HN O | Zn 2+ B R2 N Zn Erase
Clathrin coat features and activities it participated include Its protein chains, triskelion, are arranged with the membrane through adaptors to form invaginations or pits. Its protein chains, triskelion, are arranged with the membrane through adaptors to form invaginations or pits. Its protein chains, triskelion, are arranged with the membrane through adaptors to form invaginations or pits. Its protein chains, triskelion, are arranged with the membrane through adaptors to form invaginations or pits.
Configurational antrapy Molten globules Clusters of frustrated contacts Functionally siatinet states B Which is the site of folded proteins O A B
The amino acid shown below has an ionizable side chain with a pka of 4. When this amino acid is in a more basic solution (i.e., pH 11), it would resemble ionization state C and have a charge of -1 HO OH NH₂ lonization state A NH3 lonization state C HO OH NH3+ Ionization state B dyb NH₂ lonization state D
Classify each characteristic as describing glycoproteins or proteoglycans. Glycoproteins Proteoglycans Answer Bank form highly specific sites for recognition only has sulfated glycosaminoglycan chains found in Golgi complexes, secretory granules, and high-affinity binding by lectins covalently linked to Ser and lysosomes exclusively located at the cell surface may contain N-linked glycosidic bonds include the heparan sulfate family and in the extracellular matrix
Why might adding a strong reducing agent like Dithiothreitol (DTT) help denature an extracellular protein? O Disulfide bonds might be reduced that might be critical in stabilizing its structure O Disulfide bonds might be oxidized that might be critical in stabilizing its structure O Disulfide bonds formed inside the cytoplasm can be oxidized O Cysteines can be reduced to form stabilizing disulfide bonds
NAZO NHZ Ala-Cys-Glu -Tyr - Trp - Lys - Arg - His -Pro-G ly Glu pka 4.15 SH Tyr 10.10 Draw Charges Lys 10.67 Olt A3 12.10 +NH₂ Ntrm 2) Calculate net charge 3) write out I letter code 300 Ctim 3 juli of peptich (above) Ⓒ pH; 1,7,12
wnich snows tne specinicity pockets. The S pocket nas a Ra glutamic acid in the bottom, the S2 pocket is small and hydrophobic, and the S,' pocket is deep and hydrophobic. Suggest a 3-amino acid sequence that this protease would R2 H cleave and indicate between which sites the peptide bond would be broken. S2 Which sequence would this protease cleave? Val-Lys-Phe Phe-Lys-Val Lys-Phe-Val Val-Phe-Lys Phe-Val-Lys O Lys-Val-Phe The peptide bond that is broken is between which sites? O S2 and S,' OS, and S,' O S2 and S1 O S2 and S1, and S and S,' IZ