9. The T conformation of the hemoglobin tetramer is stabilized (in part) by a saltlinkage between the side chain of the lysine residue at position 40 in the a-chainof one aß dimer and the C-terminal carboxylate group of the ß-chain of theopposing aß dimer. Draw a diagram of this salt linkage (show complete sidechains).

Answered: 9. The T conformation of the hemoglobin…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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9. The T conformation of the hemoglobin tetramer is stabilized (in part) by a salt
linkage between the side chain of the lysine residue at position 40 in the a-chain
of one aß dimer and the C-terminal carboxylate group of the ß-chain of the
opposing aß dimer. Draw a diagram of this salt linkage (show complete side
chains).

Expert Solution

Step 1: Structure of Hemoglobin

Hemoglobin is a globular protein, ie it is roughly spherical. It is a tetramer of two types of protein: α chain and β chain (this has nothing to do with alpha helix or beta sheets, the two polypeptide chains are labelled α and β). The α and β chains interact with one another to form a dimer (α1 β1) that interacts with another dimer (α2 β2) to form the tetramer.

There are two conformations in which hemoglobin can exist: R state and T state. R state has a higher affinity for oxygen. When oxygen is absent, hemoglobin exists in the T state. When oxygen binds to hemoglobin in the T state, it induces a change in conformation, from the T state to the R state.