The document discusses the Hill equation, which describes cooperative ligand binding to multisubunit proteins like hemoglobin. The Hill equation models how the binding of oxygen to one subunit of hemoglobin affects the binding of oxygen to other subunits. Archibald Hill first analyzed cooperative oxygen binding to hemoglobin in 1910. The Hill equation takes the form of an expression relating the fraction of binding sites occupied to the ligand concentration.
2. Hill equation
Cooperative binding of a ligand to a
multimeric protein is a form of allosteric
binding often observed in multimeric
proteins .such as we observe with the
binding of O2 to hemoglobin,
Cooperative binding of oxygen by
hemoglobin was first analyzed by
Archibald Hill in 1910. From this work
came a general approach to the study of
cooperative ligand binding to
multisubunit proteins.
3. Hill equation
For a protein with n binding sites, the equilibrium of the
reversible binding of a protein (P) to a ligand(L)
Equation becomes
P + nL PLn 1
and the expression for the association constant
becomes
[PLn]
Ka =-------------2
[P][L]n
4. Hill equation
The expression for 慮 is,,
[L]n where, binding sites
occupied
慮 = ---------- 3 慮=--------------------
--
[L]n + Kd total binding sites
Rearranging, then taking the log of both sides, yields
慮 [L]n
---------= ----- .4
1 慮 Kd
慮
log(---------) = n log[L] logKa 5
1 慮
Equation 5 is the Hill equation
5. Allosteric protein
An allosteric protein is one in which the binding
of a ligand to one site affects the binding
properties of another site on the same protein.
Such as hemoglobin, myoglobin etc.
Hemoglobin (Mr 64,500; abbreviated Hb) is
roughly spherical, with a diameter of nearly 5.5
nm. It is a tetrameric protein containing four
heme prosthetic groups, one associated with each
polypeptide chain.