Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN: 9780134580999
Author: Elaine N. Marieb, Katja N. Hoehn
Publisher: PEARSON
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- Is there anyway to draw a visual diagram for this as the explanation does not make sense how can 2 aspartates interact with each other under physiological pH?arrow_forwardATP Synthase contains with in it one of the most conserved residues in a protein we know. Asp 61. This is the amino acid that carries the proton. a. Why would this residue be so highly conserved? What would happen if a mutation occurred that would change Asp to Ala? b. At the end of one spin of ATP synthase when the proton is in a position to leave to the intermembrane space the Asp comes into close contact with another very highly conserved residue Arg 210. Explain how this Arg residue could help the proton attached to Asp to leave. Hint think pKa Answer both parts with good explanationarrow_forwardWhat is the role of tyrosine in prostaglandin synthesis? Tyrosine provides the proton to the double bond initiating the cascade for ring formation. Tyrosine is the source of the hydroxyl groups that converts PGH to PGD2 and PGF. Tyrosine provides a hydrogen free radical that initiates the cascade synthesizing the prostaglandins. Tyrosine provides hydrogen bonding interaction that immobilizes arachidonic acid for conversion by cyclooxygenases (COX) Tyrosine is a catalytic residue at the active site of COX.arrow_forward
- Some proteins may be phosphorylated by enzymes called kinases. Which of the following statements best describes this type of post-translational modification (PTM)? Phosphorylation is an irreversible modification of an amino acid side chain in the protein. Phosphorylation is a reversible modification of an amino acid side chain in the protein. Phosphorylation is an irreversible modification of the peptide backbone. Phosphorylation is a reversible modification of the peptide backbone.arrow_forwardWhat are some of the interactions made between ATP and the kinase? Describe bonds that the protein makes with each of the following: the phosphate groups the sugar the adenine basearrow_forwardIn the normal cycle of Ras activity, when Ras is bound to y activity that removes a phosphate to convert GTP back to GDP and this it is inactive. Activation of Ras involves exchanging GDP for The Ras protein has intrinsic Ras. inactivates activates ATP GTP «< Questic A Moving to another question will save this response. ADP GDP GTPase Clo nucleasearrow_forward
- A peptide with the sequence AELQAKSAIAHELQAKAAIAHA is treated with ATP while in the presence of kinase An alpha helix is formed with the phosphorylated at pH 5 In the direction of the helix axis, what is the length of the helixarrow_forwardWhich of the following would result in an increase in the amount of F-2,6-BP? (select all that apply) Group of answer choices high blood glucose activation of fructose bisphosphatase 2 increased phosphofructokinase 2 activity increased glucagon secretion increased phosphorylation of the bifunctional enzymearrow_forwardS-adenosylmethionine is an activated carrier molecule that transfers which of the following groups? the carboxylic acid group (with one carbon) the phosphate group (with zero carbons) the glucose group (with six carbons) the methyl group (with one carbon) the acetyl group (with two carbons)arrow_forward
- Endothelial cells lining blood vessels can produce large amounts of nitric oxide (NO). The NO diffuses out of the endothelial cells and into smooth muscle cells that are in close proximity. In the smooth muscle cells, NO binds to an enzyme, X, to rapidly increase intracellular levels of Y. Y causes rapid relaxation of smooth muscle cells surrounding the blood vessels. The actions of the Y molecule are controlled by enzyme Z which degrades protein Y into a non-functional form, blocking vasoconstriction and retaining high blood flow. Identify molecules X, Y and Z and explain how the drug Viagra targets this pathway.arrow_forward5) The disease Phenylketonuria (or PKU) occurs when the enzyme that helps to catalyze the conversion of the amino acid phenylalanine into non-harmful tyrosine is mutated and doesn't work as well (or at all). Phenylalanine will still break down into tyrosine by itself, because this is a favorable reaction. Why is the non-functional enzyme a problem? Explain in a few sentences. al.H.colbe91srtihot wolsd sldu non lom i anolterineon mundillups betsmus 8880arrow_forwardI'm a bit confused about this question will someone help me understand the conceptarrow_forward
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