Lecture13 - BCH 227 FALL 2010 LECTURE 13: COOPERATIVITY...

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1 Cooperativity, Allostery and Functional Regulation BIOCHEM 227 FALL 2010 Lecture 13 Monday, September 27, 2010 TODAY • Structures of examples from last week • Principles of cooperativity and allostery •H emog lob in • Aspartate transcarbamoylase • Covalent regulation of protein function BCH 227 FALL 2010 LECTURE 13: COOPERATIVITY & ALLOSTERY 27 SEP 2010
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2 Enzyme Examples: Structures Cooperativity and Allostery BCH 227 FALL 2010 LECTURE 13: COOPERATIVITY & ALLOSTERY 27 SEP 2010
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3 Binding of Ligands Binding is the reversible (typically noncovalent) specific association of a protein and another molecule Ligand = that which is bound Binding site = where this happens on the protein Binding interface = where the two meet, and the interactions that hold them together Binding of Ligands BCH 227 FALL 2010 LECTURE 13: COOPERATIVITY & ALLOSTERY 27 SEP 2010
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4 Binding of Ligands Motions on Binding • Binding can affect structures – altering of conformational equilibria •Ex amp l e s – Enzyme active site – Sidechain reconfiguration – Hinged domains –Induced fo ld ing BCH 227 FALL 2010 LECTURE 13: COOPERATIVITY & ALLOSTERY 27 SEP 2010
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5 “Induced Fit” • “Induced fit” vs. “conformational selection” Cooperativity & Allostery • Cooperativity – when multiple binding sites are present for a
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This note was uploaded on 12/19/2010 for the course BIOCHEM 227 taught by Professor Coggins during the Fall '10 term at Duke.

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Lecture13 - BCH 227 FALL 2010 LECTURE 13: COOPERATIVITY...

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