Fundamentals of Biochemistry: Life at the Molecular Level 5th Edition

Published by Wiley
ISBN 10: 1118918401
ISBN 13: 978-1-11891-840-1

Chapter 9 - Lipids and Biological Membranes - Exercises - Page 290: 17

Answer

a) A Helices have 3.6 residues per turn with a pitch of 5.4 residues. Hence they have a rise per residue of (5.4 A/turn)/(3.6 residues/turn) = 1.50 A. It therefore requires an a helix of 30 A/1.50 A = 20 residues to span the hydrocarbon bilayer core. b) ß sheets have a length of 3.5 A per residue. The length of a ß sheet required to span the 30-A wide hydrocarbon core of a lipid bilayer when it is inclined by 30° to the membrane normal is 30 A/cos 30º = 34.6 A. Hence the number of residues in this ß strand is 34.6 A/3.5A - 10 residues. c) Besides penetrating the hydrocarbon core of a bilayer, the transmembrane element of a polypeptide must also pass through the flanking layers of head groups. These layers have relatively few hydrogen bonding groups and hence the polypeptide strand continue their a helical or ß. The additional residues form a helix, which partially satisfies backbone hydrogen bonding requirements, where the lipid head groups do not offer hydrogen bonding partners.

Work Step by Step

a) A Helices have 3.6 residues per turn with a pitch of 5.4 residues. Hence they have a rise per residue of (5.4 A/turn)/(3.6 residues/turn) = 1.50 A. It therefore requires an a helix of 30 A/1.50 A = 20 residues to span the hydrocarbon bilayer core. b) ß sheets have a length of 3.5 A per residue. The length of a ß sheet required to span the 30-A wide hydrocarbon core of a lipid bilayer when it is inclined by 30° to the membrane normal is 30 A/cos 30º = 34.6 A. Hence the number of residues in this ß strand is 34.6 A/3.5A - 10 residues. c) Besides penetrating the hydrocarbon core of a bilayer, the transmembrane element of a polypeptide must also pass through the flanking layers of head groups. These layers have relatively few hydrogen bonding groups and hence the polypeptide strand continue their a helical or ß. The additional residues form a helix, which partially satisfies backbone hydrogen bonding requirements, where the lipid head groups do not offer hydrogen bonding partners.
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