A typical integral membrane protein has a stretch (or stretches) of ~20 hydrophobic aminoacids that form an α-helix that spans the bilayer (as is found in membrane proteins such asglycophorin A and bacteriorhodopsin). Compare and contrast the molecular and structural features of gramicidin with a membrane-spanning α-helix. Explain how gramicidin can forman ion channel when a typical membrane-spanning α-helix cannot (eg, glycophorin A).
A typical integral membrane protein has a stretch (or stretches) of ~20 hydrophobic aminoacids that form an α-helix that spans the bilayer (as is found in membrane proteins such asglycophorin A and bacteriorhodopsin). Compare and contrast the molecular and structural features of gramicidin with a membrane-spanning α-helix. Explain how gramicidin can forman ion channel when a typical membrane-spanning α-helix cannot (eg, glycophorin A).
Biochemistry
6th Edition
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Reginald H. Garrett, Charles M. Grisham
Chapter32: The Reception And Transmission Of Extracellular Information
Section: Chapter Questions
Problem 11P
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A typical integral membrane protein has a stretch (or stretches) of ~20 hydrophobic amino
acids that form an α-helix that spans the bilayer (as is found in membrane proteins such as
glycophorin A and bacteriorhodopsin). Compare and contrast the molecular and structural
acids that form an α-helix that spans the bilayer (as is found in membrane proteins such as
glycophorin A and bacteriorhodopsin). Compare and contrast the molecular and structural
features of gramicidin with a membrane-spanning α-helix. Explain how gramicidin can form
an ion channel when a typical membrane-spanning α-helix cannot (eg, glycophorin A).
an ion channel when a typical membrane-spanning α-helix cannot (eg, glycophorin A).
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