CHAPTER 5 - BINDING
C: MODEL BINDING SYSTEMS
BIOCHEMISTRY - DR. JAKUBOWSKI
3/29/16
Learning Goals/Objectives for Chapter 5C: After class and
this reading, students will be able to
- explain the similarities and differences in structure
between myoglobin and hemoglobin in the deoxy and oxy states
- state structural features of Hb that stabilizes the
deoxystate and the oxystate
- draw graphs of fractional saturation Y vs L (or pO2) for Mb
and Hb (at different pHs and in the presence of CO2 for Hb) and
explain their apparent similarities and differences
- draw a thermodynamic cycle for the interactions of O2, CO2
and H+ with deoxy-Hb and oxy-Hb
- explain how Hill Plot analysis can account for cooperative
binding curves for Hb.
- give a simple explanation of the MWC model and draw cartoon
representations of Hb in the T and R state, describing the
characteristics of those states
- given definitions of the MWC parameters (L, KT, KR, c, and
α) and the assumptions of the model, explain how this model
accounts for cooperative sigmoidal binding curves for Hb and
dioxygen.
- draw cartoon models and explain differences in lock and key,
induced fit, and conformational selection as mechanisms for
ligand bind.
- Explain biological advantages elicited on ligand binding by
intrinsically disordered proteins
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C1.
Myoglobin, Hemoglobin, and their Ligands
C2.
Normal and Cooperative Binding of Dioxygen
C3.
Mathematical Analysis of Cooperative Binding - Hill Plot
C4.
Mathematical Analysis of Cooperative Binding - MWC Symmetry
Model
C5.
Mathematical Analysis of Cooperative Binding - KNF Sequential
Model
C6.
Conformational Selection
C7.
Binding to Intrinsically Disorder Protein and MORFs
C8.
Binding, Intracellular Granules
and Droplets
updated and new title
C9.
Binding and Linked Equilibria
C10.
Macromolecule
Oligomer Formation
and Symmetry
C11.
Conformational and Binding - Examples
C12.
Free Energy and Cooperativity
C13.
Links and References
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Model Binding Systems
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