Lecture14 - BCH 227 FALL 2010 LECTURE 14: COOPERATIVITY...

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1 Cooperativity, Allostery and Functional Regulation BIOCHEM 227 FALL 2010 Lecture 14 Wednesday, September 29, 2010 TODAY • Continued: Hemoglobin • Aspartate transcarbamoylase • Covalent regulation of protein function BCH 227 FALL 2010 LECTURE 14: COOPERATIVITY & ALLOSTERY CONTINUED 29 SEP 2010
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2 Myoglobin O 2 Binding θ = fraction bound Myoglobin O 2 Binding PL PL L L d d K K ⎡ ⎤⎡ ⎤ ⎣ ⎦⎣ ⎦ = ⎡ ⎤ ⎣ ⎦ = + ⎡⎤ ⎣⎦ BCH 227 FALL 2010 LECTURE 14: COOPERATIVITY & ALLOSTERY CONTINUED 29 SEP 2010
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3 Hemoglobin O 2 Binding Hemoglobin T & R States T state = low affinity R state = high affinity BCH 227 FALL 2010 LECTURE 14: COOPERATIVITY & ALLOSTERY CONTINUED 29 SEP 2010
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4 Cooperative Transition •B ind ing o f f i r s t O 2 to one subunit in T state is hard • Binding of last O 2 to the fourth subunit in R state is easy • At some point, T → R transition happens – Conformation changes propagated to interfaces Cooperative Transition BCH 227 FALL 2010 LECTURE 14: COOPERATIVITY & ALLOSTERY CONTINUED 29 SEP 2010
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Lecture14 - BCH 227 FALL 2010 LECTURE 14: COOPERATIVITY...

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