bis102-10-12-lec9

bis102-10-12-lec9 - 10-12-2011 Lecture 9 Tertiary...

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10-12-2011 Lecture 9 Tertiary structure: myoglobin- stores oxygen in muscles - obeys normal saturation type of curve. Quaternary Structure: -conformation caused by proteins. - hemoglobin- has both tertiary and quaternary structure - transport oxygen from the lungs to the tissues. -sigmoidal curve (S shaped curve) - suggests that theres an interaction between the sites of the protein. .. binding of the oxygen at one site on the tetramer increases the likelihood that oxygen binds at the remaining unoccupied sites. proximal histidine residue binds to the 5th coordination site on the iron. before oxygen-- the iron is hanging from the ring. .. but when oxygen is added. .. the iron is at the center of the ring. oxygen binds to the 6th coordination site of the iron. resonance occurs between the 2 structures when oxygen is bound to iron. when oxygen is bound to myoglobin, another histidine, called the distal histidine, forms a hydrogen bond with the bound oxygen.
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This note was uploaded on 01/15/2012 for the course BIS 102 taught by Professor Hilt during the Fall '08 term at UC Davis.

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bis102-10-12-lec9 - 10-12-2011 Lecture 9 Tertiary...

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