nya22 Posted October 15, 2008 Share Posted October 15, 2008 Q. Hemoglobin is a tetrameric protein with two alpha and two beta polypeptide subunits. The structures of the alpha and beta subunits are remarkably similar to that of myoglobin. Myoglobin is also a heme containing protein that binds oxygen that has a structure that is similar to that of hemoglobin. However at a number of positions, hydrophilic residues in myoglobin have been replaced by hydrophobic residues in hemoglobin on the outside of the individual subunits. a. How can this observation be reconciled with the generaliztion that hydrophobic residues fold into the interior of proteins? b. In this regard, what can you say about the nature of the interactions that determine the quaternary structure of hemoglobin? Link to comment Share on other sites More sharing options...
CharonY Posted October 15, 2008 Share Posted October 15, 2008 What precisely do you need help with? What is it that you understand/do not understand? Link to comment Share on other sites More sharing options...
nya22 Posted October 15, 2008 Author Share Posted October 15, 2008 Its a question we received as a part of homework and I can't figure it out. I dn't understand what the question is asking and how to go about answering it. For some reason I a m finding this chapter difficult Link to comment Share on other sites More sharing options...
MedGen Posted October 16, 2008 Share Posted October 16, 2008 The key to it is considering the position of the hydrophobic aa's and the quaternary structure, if that helps at all. Link to comment Share on other sites More sharing options...
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